Skip to main content

Part of the book series: Reviews of Physiology, Biochemistry and Pharmacology ((REVIEWS,volume 82))

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Abbreviations

ATP:

adenosine triphosphate

DNP:

dinitrophenol

dpm:

disintegrations per minute

GTP:

guanosine triphosphate

mRNA:

messenger ribonucleic acid

PEP:

phosphoenol pyruvate

RNA:

ribonucleic acid

Tris:

Tris(hydroxymethyl)aminomethane

tRNA:

transfer ribonucleic acid

References

  • Abdel-Samie, Y.M., Broda, E., Kellner, G.: The autonomous production of individual serum proteins by tissue in culture. Biochem. J. 75, 209–215 (1960)

    Google Scholar 

  • Abdel-Samie, Y., Broda, E., Kellner, G., Zischka, W.: Production of serum albumin and of globulins by chick mesenchymal tissue and by HeLa tumour tissue in culture. Nature (Lond.) 184, 361–362 (1959)

    Google Scholar 

  • Airhart, J., Vidrich, A., Khairallah, E.A.: Compartmentation of free amino acids for protein synthesis in rat liver. Biochem. J. 140, 539–548 (1974)

    Google Scholar 

  • Askonas, B.A., Campbell, P.N., Humphrey, J.H., Work, T.S.: The source of antibody globulin in rabbit milk and goat colostrum. Biochem. J. 56, 597–601 (1954)

    Google Scholar 

  • Bancroft, F.C., Levine, L., Tashjian, A.H., Jr.: Serum albumin production by hepatoma cells in culture: direct evidence for stimulation by hydrocortisone. Biochem. Biophys. Res. Commun. 37, 1028–1035 (1969).

    Google Scholar 

  • Baraona, E., Leo, M.A., Borowsky, S.A., Lieber, C.S.: Alcoholic hepatomegaly: accumulation of protein in the liver, Science 190, 794–795 (1975)

    Google Scholar 

  • Bayly, R.J., Evans, E.A.: Stability and storage of compounds labelled with radioiso-topes. J. Labelled Comp. 2, 1–34 (1966)

    Google Scholar 

  • Becker, F.F., Klein, K.M., Asofsky, R.: Plasma protein synthesis by N-2-Fluorenyl-acetamide-induced primary hepatocellular carcinomas and hepatic nodules. Cancer Res. 32, 914–920 (1972)

    Google Scholar 

  • Bellamy, G., Bornstein, P.: Evidence for procollagen, a biosynthetic precursor of collagen. Proc. Natl. Acad. Sci. USA 68, 1138–1142 (1971)

    Google Scholar 

  • Birken, S., Smith, D.L., Canfield, R.E., Boime, I.: Partial amino acid sequence of human placental lactogen precursor and its mature hormone form produced by membrane-associated enzyme activity. Biochem. Biophys. Res. Commun 74, 106–112 (1977)

    Google Scholar 

  • Bissell, M.J., Tosi, R., Gorini, L.: Mechanism of excretion of a bacterial proteinase: factors controlling accumulation of the extracellular proteinase of a Sarcina strain (Coccus P). J. Bacteriol. 105, 1099–1109 (1971)

    Google Scholar 

  • Blair, G.E., Ellis, R.J.: Protein synthesis in chloroplasts I. Light-driven synthesis of the large subunit of fraction I protein by isolated pea chloroplasts. Biochim. Biophys. Acta 319, 223–234 (1973)

    Google Scholar 

  • Blobel, G., Dobberstein, B.: Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67, 835–851 (1975)

    Google Scholar 

  • Blobel, G., Sabatini, D.D.: Ribosome — membrane interaction in eukaryotic cells. Biomembranes 2, 193–195 (1971)

    Google Scholar 

  • Bocci, V.: Metabolism of plasma proteins (Review). Arch. Fisiol. 67, Fasc. IV, 315–444 (1970)

    Google Scholar 

  • Bogorad, L.: Evolution of organelles and eukaryotic genomes. Science 188, 891–898 (1975)

    Google Scholar 

  • Braatz, J.A., Heath, E.C.: The role of polysaccharide in the secretion of protein by Micrococcus sodonensis. J. Biol. Chem. 249, 2536–2547 (1974)

    Google Scholar 

  • Braun, G.A., Marsh, J.B., Drabkin, D.L.: Stimulation of protein and plasma albumin synthesis in a cell-free system from livers of nephrotic rats. Biochem. Biophys. Res. Commun. 8, 28–32 (1962a)

    Google Scholar 

  • Braun, G.A., Marsh, J.B., Drabkin, D.L.: Synthesis of plasma albumin and tissue proteins in regenerating liver. Metabolism 11, 957–966 (1962b)

    Google Scholar 

  • Breslow, J.L., Sloan, H.R., Ferrans, V.J., Anderson, J.L., Levy, R.I.: Characterization of the mouse liver cell line F L 83 B. Exp. Cell Res. 78, 441–453 (1973)

    Google Scholar 

  • Bretscher, M.S.: Phosphatidyl-ethanolamine: differential labelling in intact cells and cell ghosts of human erythrocytes by a membrane-impermeable reagent. J. Mol. Biol. 71, 523–528 (1972)

    Google Scholar 

  • Bretscher, M.S.: C-terminal region of the major erythrocyte sialoglycoprotein is on the cytoplasmic side of the membrane. J. Mol. Biol. 98, 831–833 (1975)

    Google Scholar 

  • Brunish, R., Luck, J.M.: Amino acid “incorporation” in vitro by desoxypentose nucleoprotein and histone. J. Biol. Chem. 197, 869–882 (1952)

    Google Scholar 

  • Burstein, Y., Kantor, F., Schechter, I.: Partial amino-acid sequence of the precursor of an immunoglobulin light chain containing NH2-terminal pyroglutamic acid. Proc. Natl. Acad. Sci. USA 73, 2604–2608 (1976)

    Google Scholar 

  • Burstein, Y., Schechter, I.: Amino acid-sequence variability at the N-terminal extra piece of mouse immunoglobulin light-chain precursors of the same and different subgroups. Biochem. J. 157, 145–151 (1976)

    Google Scholar 

  • Burstein, Y., Schechter, I.: Amino acid sequence of the NH2-terminal extra piece segments of the precursors of mouse immunoglobulin λ1-type and κ-type light chains. Proc. Natl. Acad. Sci. USA 74, 716–720 (1977)

    Google Scholar 

  • Butterworth, B.E., Hall, L., Stoltzfus, CM., Rueckert, R.R.: Virus-specific proteins synthesized in encephalomyocarditis virus-infected HeLa cells. Proc. Natl. Acad. Sci. USA 68, 3083–3087 (1971)

    Google Scholar 

  • Campbell, P.N.: The correlation between morphological structure and the synthesis of serum albumin by the microsome fraction of the rat liver cell. In: Biological Structure and Function. Goodwin, T.W., Lindberg, O. (eds.), Vol. I, pp. 255–259. London—New York: Academic Press 1961a

    Google Scholar 

  • Campbell, P.N.: The synthesis of serum albumin by the microsome fraction of the liver. In: Protein Biosynthesis. Harris, R.J.C. (ed.), pp. 19–35. New York—London: Academic Press 1961b

    Google Scholar 

  • Campbell, P.N.: The Biosynthesis of Rat Serum Albumin. Proc. 5th Internatl. Congr. Biochem., Moscow 1961c, Vol. II, pp. 195–203

    Google Scholar 

  • Campbell, P.N.: The correlation between morphology and protein synthesizing activity in liver. Acta Biol. Med. Germanica 19, 621–639 (1967)

    Google Scholar 

  • Campbell, P.N.: Functions of polyribosomes attached to membranes of animal cells. FEBS Lett. 7, 1–7 (1970)

    Google Scholar 

  • Campbell, P.N.: The biosynthesis of serum albumin. FEBS Lett. 54, 119–121 (1975)

    Google Scholar 

  • Campbell, P.N., Greengard, O., Kernot, B.A.: Studies on the synthesis of serum albumin by the isolated microsome fraction from rat liver. Biochem. J. 74, 107–117 (1960)

    Google Scholar 

  • Campbell, P.N., Kernot, B.A.: The incorporation of [14C] leucine into serum albumin by the isolated microsome fraction from rat liver. Biochem. J. 82, 262–266 (1962)

    Google Scholar 

  • Campbell, P.N., Stone, N.E.: The synthesis of serum albumin and tissue proteins in slices of rat liver and liver tumour. Biochem. J. 66, 19–31 (1957)

    Google Scholar 

  • Chan, S.J., Keim, P., Steiner, D.F.: Cell-free synthesis of rat preproinsulins — characterization and partial amino acid sequence determination. Proc. Natl. Acad. Sci. USA 73, 1964–1968 (1976)

    Google Scholar 

  • Chandrasekharan, N., Fleck, A., Munro, H.N.: Albumin content of rat hepatic cells at different levels of protein intake. J. Nutr. 92, 497–502 (1967)

    Google Scholar 

  • Chen, R.F.: Removal of fatty acids from serum albumin by charcoal treatment. J. Biol. Chem. 242, 173–181 (1967)

    Google Scholar 

  • Clarke, D.D., Mycek, M.J., Neidle, A., Waelsch, H.: The incorporation of amines into protein. Arch. Biochem. Biophys. 79, 338–354 (1959)

    Google Scholar 

  • Cohen, S.: Turnover of some chromatographically separated serum protein fractions in the rat. S. Afr. J. Med. Sci. 23, 245–256 (1957)

    Google Scholar 

  • Cohn, D.V., Macgregor, R.R., Chu, L.L.H., Kimmel, J.R., Hamilton, J.W.: Calcemic fraction-A: biosynthetic peptide precursor of parathyroid hormone. Proc. Natl. Acad. Sci. USA 69, 1521–1525 (1972)

    Google Scholar 

  • Cornwell, D.G., Luck, J.M.: Studies on amino-acid protein interactions. Arch. Biochem. Biophys. 73, 391–409 (1958)

    Google Scholar 

  • Crane, L.J., Miller, D.L.: Synthesis and secretion of fibrinogen and albumin by isolated rat hepatocytes. Biochem. Biophys. Res. Commun. 60, 1269–1277 (1974)

    Google Scholar 

  • Crawford, J.L., Lipscomb, W.N., Schellman, C.G.: The reverse turn as a polypeptide conformation in globular proteins. Proc. Natl. Acad. Sci. USA 70, 538–542 (1973)

    Google Scholar 

  • Decken, A., von der: Labelling of immunologically specific proteins by ribonucleoprotein particles from rat-liver and chick-liver cell sap. Biochem. J. 88, 385–394 (1963a)

    Google Scholar 

  • Decken, A., von der: Labelling with 14C amino acids of albumin-like protein by rat liver ribonucleoprotein particles. J. Cell Biol. 16, 471–481 (1963b)

    Google Scholar 

  • Decken, A., von der, Campbell, P.N.: The role of soluble ribonucleic acid in the synthesis of serum albumin by the isolated microsome fraction from rat liver. Biochem. J. 80, 38P–39P (1961a)

    Google Scholar 

  • Decken, A., von der, Campbell, P.N.: Studies on the synthesis of serum albumin by isolated ribonucleoprotein particles from rat liver. Biochem. J. 80, 39P (1961b)

    Google Scholar 

  • Decken, A., von der, Campbell, P.N.: Studies on the synthesis of serum albumin by ribonucleoprotein particles isolated from rat liver. Biochem. J. 84, 449–455 (1962)

    Google Scholar 

  • Delaville, M., Delaville, G., Delaville, J.: Caractère de solubilité de la fraction albumi-nique de sérum sanguin dans les solutions d'éthanoltrichloracétique; application au dosage des diverses fractions protéiques du sérum. Ann. Biol. Clin. (Paris) 12, 320–323 (1954a)

    Google Scholar 

  • Delaville, M., Delaville, G., Delaville, J.: Caractère de solubilité de la fraction albumi-nique du s érum sanguin dans l'alcool trichloracétique; son application au dosage des diverses fractions protéiques. Ann. Pharm. Fr. 12, 109–113 (1954b)

    Google Scholar 

  • Deschatrette, J., Weiss, M.C.: Characterization of differentiated and dedifferentiated clones from a rat hepatoma. Biochimie 56, 1603–1611 (1974)

    Google Scholar 

  • Devillers-Thiery, A., Kindt, T., Scheele, G., Blobel, G.: Homology in amino-terminal sequence of precursors to pancreatic secretory proteins. Proc. Natl. Acad. Sci. USA 72, 5016–5020 (1975)

    Google Scholar 

  • Dobberstein, B., Blobel, G., Chua, N.-H.: In vitro synthesis and processing of a putative precursor for the small subunit of ribulose-l,5-biphosphate carboxylase of Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 74, 1082–1085 (1977)

    Google Scholar 

  • Dorling, P.R., Quinn, P.S., Judah, J.D.: Evidence for the coupling of biosynthesis and secretion of serum albumin in the rat. The effect of colchicine on albumin production. Biochem. J. 152, 341–348 (1975)

    Google Scholar 

  • Drabkin, D.L., Marsh, J.B.: Metabolic channeling in experimental nephrosis. I. Protein and carbohydrate metabolism. J. Biol. Chem. 212, 623–631 (1955)

    Google Scholar 

  • Eagle, H., Oyama, V.I., Piez, K.A.: The reversible binding of half-cysteine residues to serum protein and its bearing on the cysteine requirement of cultured mammalian cells. J. Biol. Chem. 235, 1719–1726 (1960)

    Google Scholar 

  • Edman, P., Begg, G.: A protein sequenator. Eur. J. Biochem. 1, 80–91 (1967)

    Google Scholar 

  • Edwards, K.: Biosynthesis of albumin in rat liver. Ph. D. Thesis, University of Melbourne, 1978

    Google Scholar 

  • Edwards, K., Fleischer, B., Dryburgh, H., Fleischer, S., Schreiber, G.: The distribution of albumin precursor protein and albumin in liver. Biochem. Biophys. Res. Commun. 72, 310–318 (1976a)

    Google Scholar 

  • Edwards, K., Schreiber, G., Dryburgh, H., Millership, A., Urban, J.: Biosynthesis of albumin via a precursor protein in Morris hepatoma 5123TC. Cancer Res. 36, 3113–3118 (1976b)

    Google Scholar 

  • Edwards, K., Schreiber, G., Dryburgh, H., Urban, J., Inglis, A.S.: Synthesis of albumin via a precursor protein in cell suspensions from rat liver. Eur. J. Biochem. 63, 303–311 (1976c)

    Google Scholar 

  • Faber, A.J., Miall, S.H., Tamaoki, T.: Synthesis of albumin with exogenous mouse-liver messenger RNA in a homologous cell-free system. Can. J. Biochem. 52, 429–432 (1974)

    Google Scholar 

  • Fairclough, G.F., Fruton, J.S.: Peptide-protein interaction as studied by gel filtration. Biochemistry 5, 673–683 (1966)

    Google Scholar 

  • Feldmann, G., Penaud-Laurencin, J., Crassous, J., Benhamou, J.P.: Albumin synthesis by human liver cells: its morphological demonstration. Gastroenterology 63, 1036–1048 (1972)

    Google Scholar 

  • Fernandez, A., Sobel, C, Goldenberg, H.: An improved method for determination of serum albumin and globulin. Clin. Chem. 12, 194–205 (1966)

    Google Scholar 

  • Fishman, B., Wurtman, R.J., Munro, H.N.: Daily rhythms in hepatic polysome profiles and tyrosine transaminase activity: Role of dietary protein. Proc. Natl. Acad. Sci. USA 64, 677–682 (1969)

    Google Scholar 

  • Foster, J.F.: Plasma Albumin. In: The Plasma Proteins. Putman, F.W. (ed.), Vol. I, pp. 179–239. New York—London: Academic Press 1960

    Google Scholar 

  • Foster, J.F., Sterman, M.D.: Conformation changes in bovine plasma albumin associated with hydrogen ion and urea binding. II. Hydrogen ion titration curves. J. Am. Chem. Soc. 78, 3656–3660 (1956)

    Google Scholar 

  • Freeman, T.: The function of plasma proteins. In: Protides of the Biological Fluids. Peeters, H.(ed.), Vol. XV, pp. 1–14. Amsterdam: Elsevier 1967

    Google Scholar 

  • Freeman, T., Gordon, A.H.: Metabolism of albumin and γ-globulin in protein deficient rats. Clin. Sci. 26, 17–26 (1964)

    Google Scholar 

  • Gandolfi, E., Fabrini, G.: A new method for serum albumin determination. Ital. J. Biochem. 15, 244–249 (1966)

    Google Scholar 

  • Ganoza, M.C., Williams, C.A.: In vitro synthesis of different categories of specific proteins by membrane-bound and free ribosomes. Proc. Natl. Acad. Sci. USA 63, 1370–1376 (1969)

    Google Scholar 

  • Ganoza, M.C., Williams, C.A., Lipman, F.: Synthesis of serum proteins by a cell-free system from rat liver. Proc. Natl. Acad. Sci. USA 53, 619–622 (1965)

    Google Scholar 

  • Gaudernack, G., Rugstad, H.E., Hegna, I., Prydz, H.: Synthesis of serum proteins by a clonal strain of rat hepatoma cells. Exp. Cell Res. 77, 25–30 (1973)

    Google Scholar 

  • Geller, D.M., Judah, J.D., Nicholls, M.R.: Intracellular distribution of serum albumin and its possible precursors in rat liver. Biochem. J. 127, 865–874 (1972)

    Google Scholar 

  • Givan, A.L., Criddle, R.S.: Ribulosediphosphate carboxylase from Chlamydomonas reinhardi: purification, properties and its mode of synthesis in the cell. Arch. Biochem. Biophys. 149, 153–163 (1972)

    Google Scholar 

  • Glaumann, H.: Studies on the synthesis and transport of albumin in microsomal subfractions from rat liver. Biochim. Biophys. Acta 224, 206–218 (1970)

    Google Scholar 

  • Glaumann, H., Ericsson, J.L.E.: Evidence for the participation of the Golgi apparatus in the intracellular transport of nascent albumin in the liver cell. J. Cell Biol. 47, 555–567 (1970)

    Google Scholar 

  • Goldsworthy, P.D., McCartor, H.R., McGuigan, J.E., Peppers, G.F., Volwiler, W.: Relative albumin, transferrin, and fibrinogen synthesis rates in perfused bovine liver. Am. J. Physiol. 218, 1428–1433 (1970)

    Google Scholar 

  • Gordon, A.H.: Synthesis of plasma proteins by the perfused rat liver. Effects of protein free diet, 3′-MDAB and dimethylnitrosamine. Eur. J. Cancer 2, 19–31 (1966)

    Google Scholar 

  • Gordon, A.H., Humphrey, J.H.: Methods for measuring rates of synthesis of albumin by the isolated perfused rat liver. Biochem. J. 75, 240–247 (1960)

    Google Scholar 

  • Gordon, A.H., Humphrey, J.H.: Measurement of intracellular albumin in rat liver. Biochem. J. 78, 551–556 (1961)

    Google Scholar 

  • Goussault, Y., Sharif, A., Bourrilon, R.: Serum albumin biosynthesis and secretion by resting and lectin stimulated human lymphocytes. Biochem. Biophys. Res. Commun. 73, 1030–1035 (1976)

    Google Scholar 

  • Gray, J.C., Kekwick, R.G.O.: The synthesis of the small subunit of ribulose 1,5-bio-phosphate carboxylase in the french bean Phaseolus vulgaris. Eur. J. Biochem. 44, 491–500 (1974)

    Google Scholar 

  • Habener, J.F., Kemper, B., Potts, J.T., Jr., Rich, A.: Pre-proparathyroid hormone identified by cell-free translation of messenger RNA from hyperplastic human parathyroid tissue. J. clin. Invest. 56, 1328–1333 (1975)

    Google Scholar 

  • Haider, M., Tarver, H.: Effect of diet on protein synthesis and nucleic acid levels in rat liver. J Nutr. 99, 433–445 (1969)

    Google Scholar 

  • Hamashima, Y., Harter, J.G., Coons, A.H.: The localization of albumin and fibrinogen in human liver cells. J. Cell Biol. 20, 271–279 (1964)

    Google Scholar 

  • Hamilton, J.W., Niall, H.D., Jacobs, J.W., Keutmann, H.T., Potts, J.T., Jr., Cohn, D.V.: The N-terminal amino-acid sequence of bovine proparathyroid hormone. Proc. Natl. Acad. Sci. USA 71, 653–656 (1974)

    Google Scholar 

  • Harrap, K.R., Jackson, R.C., Riches, P.G., Smith, C.A., Hill, B.T.: The occurrence of protein-bound mixed disulfides in rat tissues. Biochim. Biophys. Acta 310, 104–110 (1973)

    Google Scholar 

  • Haselkorn, R., Rothman-Denes, L.B.: Protein synthesis. Annu. Rev. Biochem. 42, 397–438 (1973)

    Google Scholar 

  • Henshaw, E.C., Hirsch, C.A., Morton, B.E., Hiatt, H.H.: Control of protein synthesis in mammalian tissues through changes in ribosome activity. J. Biol. Chem. 246, 436–446 (1971)

    Google Scholar 

  • Hicks, S.J., Drysdale, J.W., Munro, H.N.: Preferential synthesis of ferritin and albumin by different populations of liver polysomes. Science 164, 584–585 (1969)

    Google Scholar 

  • Hirokawa, R., Ogata, K.: In vivo evidence for albumin biosynthesis in rat liver ribosomes. J. Biochem. (Tokyo) 52, 377–378 (1962)

    Google Scholar 

  • Hirokawa, R., Omori, S., Takahashi, T., Ogata, K.: The transfer of amino acid from soluble ribonucleic acid to microsomal albumin. Biochim. Biophys. Acta 49, 612–614 (1961)

    Google Scholar 

  • Hitzig, W.H.: Plasmaproteine, 2. Aufl. Berlin—Heidelberg—New York: Springer 1977

    Google Scholar 

  • Hochberg, A.A., Stratman, F.W., Zahlten, R.N., Lardy, H.A.: Artifacts in protein synthesis by mitochondria in vitro. FEBS Lett. 25, 1–7 (1972)

    Google Scholar 

  • Hoffenberg, R., Black, E., Brock J.F.: Albumin and γ-globulin tracer studies in protein depletion states. J. Clin. Invest. 45, 143–152 (1966)

    Google Scholar 

  • Hoffenberg, R., Gordon, A.H., Black, E.G.: Albumin synthesis by the perfused rat liver. A comparison of methods with special reference to the effect of dietary protein deprivation. Biochem. J. 122, 129–134 (1971)

    Google Scholar 

  • Holtzer, H., Holtzer, S.: The in vitro uptake of fluorescein labelled plasma proteins. I. Mature cells. C.R. Trav. Lab. Carlsberg 31, 373–408 (1960)

    Google Scholar 

  • Hosoda, J., Cone, R.: Analysis of T4 phage proteins, I. conversion of precursor proteins into lower molecular weight peptides during normal capsid formation. Proc. Natl. Acad. Sci. USA 66, 1275–1281 (1970)

    Google Scholar 

  • Ikehara, Y., Oda, K., Kato, K.: Conversion of proalbumin into serum albumin in the secretory vesicles of rat liver. Biochem. Biophys. Res. Commun. 72, 319–326 (1976)

    Google Scholar 

  • Ikehara, Y., Pitot, H.C.: Localization of polysome-bound albumin and serine dehydra-tase in rat liver cell fractions. J. Cell Biol. 59, 28–44 (1973)

    Google Scholar 

  • Inglis, A.S., Nicholls, P.W.: Identification of phenylthiohydantoins of amino acids by thin-layer chromatography. J. Chromatogr. 79, 344–346 (1973)

    Google Scholar 

  • Inglis, A.S., Nicholls, P.W., Roxburgh, G.M.: Acid hydrolysis of phenylthiohydantoins of amino acids. Aust. J. Biol. Sci. 24, 1247–1250 (1971)

    Google Scholar 

  • Inouye, S., Wang, S., Sekizawa, J., Halegoua, S., Inouye, M.: Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane. Proc. Natl. Acad. Sci. USA 74, 1004–1008 (1977)

    Google Scholar 

  • Isles, T.E., Jocelyn, P.C.: The reaction of protein thiol groups with some disulfides. Biochem. J. 88, 84–88 (1963)

    Google Scholar 

  • Iwanij, V., Chua, N.-H., Siekevitz, P.: The purification and some properties of ribulose-bisphosphate carboxylase and of its subunits from the green alga Chlamydomonas reinhardtii. Biochim. Biophys. Acta 358, 329–340 (1974)

    Google Scholar 

  • Jacobson, M.F., Baltimore, D.: Morphogenesis of poliovirus. I. Association of the viral RNA with coat protein. J. Mol. Biol. 33, 369–378 (1968)

    Google Scholar 

  • Jamieson, J.C., Ashton, F.E.: Studies on acute phase proteins of rat serum. IV. Pathway of secretion of albumin and α1-acid glycoprotein from liver. Can. J. Biochem. 51, 1281–1291(1973)

    Google Scholar 

  • Jeffay, H., Winzler, R.J.: The metabolism of serum proteins. II. The effect of dietary protein on the turnover of rat serum protein. J. Biol. Chem. 231, 111–116 (1958)

    Google Scholar 

  • Jefferson, L.S., Korner, A.: Influence of amino acid supply on ribosomes and protein synthesis of perfused rat liver. Biochem. J. 111, 703–712 (1969)

    Google Scholar 

  • John, D.W., Miller, L.L.: Regulation of net biosynthesis of serum albumin and acute phase plasma proteins. Induction of enhanced net synthesis of fibrinogen, α1-acid glycoprotein, α2 (acute phase)-globulin, and haptoglobin by amino acids and hormones during perfusion of the isolated normal rat liver. J. Biol. Chem. 244, 6134–6142 (1969)

    Google Scholar 

  • Jonckheer, M.H., Karcher, D.M.: Thyroid albumin. I. Isolation and characterization. J. Clin. Endocrinol. Metab. 32, 7–17 (1971)

    Google Scholar 

  • Judah, J.D., Gamble, M., Steadman, J.H.: Biosynthesis of serum albumin in rat liver. Evidence for the existence of ‘proalbumin'. Biochem. J. 134, 1083–1091 (1973)

    Google Scholar 

  • Judah, J.D., Nicholls, M.R.: Role of liver-cell potassium ions in secretion of serum albumin and lipoproteins. Biochem. J. 116, 663–669 (1970)

    Google Scholar 

  • Judah, J.D., Nicholls, M.R.: The separation of intracellular serum albumin from rat liver. Biochem. J. 123, 643–648 (1971a)

    Google Scholar 

  • Judah, J.D., Nicholls, M.R.: Biosynthesis of rat serum albumin. Biochem. J. 123, 649–655 (1971b)

    Google Scholar 

  • Jungblut, P.W.: Biosynthese von Ratten-Serumalbumin. II. Untersuchung der Synthese und Sekretion von Serumalbumin mit der isoliert durchströmten Rattenleber. Biochem. Z. 337, 285–296 (1963a)

    Google Scholar 

  • Jungblut, P.W.: Biosynthese von Ratten-Serumalbumin. III. Bildungsmechanismus der Polypeptidkette. Biochem. Z. 337, 297–302 (1963b)

    Google Scholar 

  • Kaji, H.: Further studies on the soluble amino acid incorporating system from rat liver. Biochemistry 7, 3844–3850 (1968)

    Google Scholar 

  • Kaji, H.: Amino-terminal arginylation of chromosomal proteins by arginyl-tRNA. Biochemistry 15, 5121–5125 (1976)

    Google Scholar 

  • Kaji, A., Kaji, H., Novelli, G.D.: Soluble amino acid-incorporating system. II. Soluble nature of the system and the characterization of the radioactive product. J. Biol. Chem. 240, 1192–1197 (1965)

    Google Scholar 

  • Kaji, H., Novelli, G.D., Kaji, A.: A soluble amino acid-incorporating system from rat liver. Biochim. Biophys. Acta 76, 474–477 (1963)

    Google Scholar 

  • Kallee, E., Lohss, F., Oppermann, W.: Trichloressigsäure-Aceton-Extraktion von Albu-minen aus Seren und Antigen-Antikörper-Präzipitaten. Z. Naturforsch. 12b, 777–783 (1957)

    Google Scholar 

  • Katz, J., Bonorris, G., Okuyama, S., Sellers, A.L.: Albumin synthesis in perfused liver of normal and nephrotic rats. Am. J. Physiol. 212, 1255–1260 (1967)

    Google Scholar 

  • Katz, J., Bonorris, G., Sellers, A.L.: Albumin metabolism in aminonucleoside nephrotic rats. J. Lab. Clin. Med. 62, 910–934 (1963)

    Google Scholar 

  • Katz, J., Sellers, A.L., Bonorris, G.: Plasma albumin synthesis in perfused rat liver. In: Stoffwechsel der isoliert perfundierten Leber. Staib, W., Scholz, R. (eds.). 3. Konfe-renz der Gesellschaft für Biologische Chemie vom 27.-29 April 1967, pp. 100–108. Berlin—Göttingen—Heidelberg: Springer 1968

    Google Scholar 

  • Kawashima, N., Wildman, S.G.: Fraction I protein. Annu. Rev. Plant Physiol. 21, 325–358 (1970)

    Google Scholar 

  • Kellenberger, E., Kellenberger-van der Kamp, C.: On a modification of the gene product P23 according to its use as subunit of either normal capsids of phage T4 or of polyheads. FEBS Lett. 8, 140–144 (1970)

    Google Scholar 

  • Keller, G.H., Taylor, J.M.: Effect of hypophysectomy on the synthesis of rat liver albumin. J. Biol. Chem. 251, 3768–3773 (1976)

    Google Scholar 

  • Kelman, L., Saunders, S.J., Frith, L., Wicht, S., Corrigal, A.: Effects of dietary protein restriction on albumin synthesis, albumin catabolism, and the plasma aminogram. Am. J. Clin. Nutr. 25, 1174–1178 (1972a)

    Google Scholar 

  • Kelman, L., Saunders, S.J., Wicht, S., Frith, L., Corrigal, A., Kirsch, R.E., Terblanche, J.: The effects of amino acids on albumin synthesis by the isolated perfused rat liver. Biochem. J. 129, 805–809 (1972b)

    Google Scholar 

  • Kemper, B., Habener, J.F., Ernst, M.D., Potts, J.T., Jr., Rich, A.: Pre-proparathyroid hormone: analysis of radioactive tryptic peptides and amino acid sequence. Biochemistry 15, 15–19 (1976)

    Google Scholar 

  • Kemper, B., Habener, J.F., Potts, J.T., Jr., Rich, A.: Proparathyroid hormone: identification of a biosynthetic precursor to parathyroid hormone. Proc. Natl. Acad. Sci. USA 69, 643–647 (1972)

    Google Scholar 

  • Kernoff, L.M., Pimstone, B.L., Solomon, J., Brock, J.F.: The effect of hypophysectomy and growth hormone replacement on albumin synthesis and catabolism in the rat. Biochem. J. 124, 529–535 (1971)

    Google Scholar 

  • Keston, A.S., Katchen, B.: Incorporation of glycine-2-C14 into homologous antibody by rabbit tissue slices. J. Immunol. 76, 253–258 (1956)

    Google Scholar 

  • Kiehn, E.D., Holland, J.J.: Synthesis and cleavage of enterovirus polypeptides in mammalian cells. J. Virol. 5, 358–367 (1970)

    Google Scholar 

  • King, T.P.: On the sulfhydryl group of human plasma albumin. J. Biol. Chem. 236, PC5 (1961)

    Google Scholar 

  • King, T.P., Spencer, M.: Structural studies and organic ligand-binding properties of bovine plasma albumin. J. Biol. Chem. 245, 6134–6148 (1970)

    Google Scholar 

  • Kirsch, J.A.W., Wise, R.W., Oliver, I.T.: Post-albumin, a foetal-specific rat plasma protein. Biochem.J. 102, 763–766 (1967)

    Google Scholar 

  • Kirsch, R., Frith, L., Black, E., Hoffenberg, R.: Regulation of albumin synthesis and catabolism by alteration of dietary protein. Nature (Lond.) 217, 578–579 (1968)

    Google Scholar 

  • Kirsch, R.E., Saunders, S.J., Frith, L., Wicht, S., Kelman, L., Brock, J.F.: Plasma amino acid concentration and the regulation of albumin synthesis. Am. J. Clin. Nutr. 22, 1559–1562 (1969)

    Google Scholar 

  • Koga, K., Tamaoki, T.: Developmental changes in the synthesis of α-fetoprotein and albumin in the mouse liver. Cell-free synthesis by membrane-bound polyribosomes. Biochemistry 13, 3024–3028 (1974)

    Google Scholar 

  • Korner, A.: Incorporation of radioactive amino acids into serum albumin by isolated rat-liver ribosomes. Biochem. J. 76, 59P–60P (1960)

    Google Scholar 

  • Korner, A., Debro, J.R.: Solubility of albumin in alcohol after precipitation by tri-chloroacetic acid. A simplified procedure for separation of albumin. Nature (Lond.) 178, 1067 (1956)

    Google Scholar 

  • Kritzman, M.G., Sukhareva, B.S., Konikuva, A.S.: Sites of incorporation of phenylala-nine labelled with carbon-14 into insulin and its chain B in vitro. Nature (Lond.) 195, 600–602 (1962)

    Google Scholar 

  • Kukral, J.C., Kerth, J.D., Pancner, R.J., Cromer, D.W., Henegar, G.C.: Plasma protein synthesis in the normal dog and after total hepatectomy. Surg. Gynecol. Obstet. 113, 360–372 (1961)

    Google Scholar 

  • Kuntz, I.D.: Protein folding. J. Am. Chem. Soc. 94, 4009–4012 (1972)

    Google Scholar 

  • Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T 4. Nature (Lond.) 227, 680–685 (1970)

    Google Scholar 

  • LeBouton, A.V.: Precursor-product relationship between intrahepatic albumin and plasma albumin. Biochem. J. 106, 503–506 (1968)

    Google Scholar 

  • Le Marchand, Y., Singh, A., Assimacopoulos-Jeannet, F., Orci, L., Rouiller, C, Jean-renaud, B.: A role for the microtubular system in the release of very low density lipoproteins by perfused mouse livers. J. Biol. Chem. 248, 6862–6870 (1973)

    Google Scholar 

  • Ledford, B.E., Papaconstantinou, J.: Regulation of albumin synthesis in cultured mouse hepatoma cells. Fed. Proc. 32, 615 (1973)

    Google Scholar 

  • Ledford, B.E., Warner, R.W., Cochran, R.A.: Albumin synthesis in cultured hepatoma cells — regulation by essential amino acids. Biochim. Biophys. Acta 475, 90–95 (1977)

    Google Scholar 

  • Leibowitz, M.J., Soffer, R.L.: Enzymatic modification of proteins. III. Purification and properties of a leucyl, phenylalanyl transfer ribonucleic acid-protein transferase from Escherichia coli. J. Biol. Chem. 245, 2066–2073 (1970)

    Google Scholar 

  • Leibowitz, M.J., Soffer, R.L.: Enzymatic modification of proteins. VII. Substrate specificity of leucyl, phenylalanyltransfer ribonucleic acid-protein transferase. J. Biol. Chem. 246, 5207–5212 (1971)

    Google Scholar 

  • Levine, S.: Solubilization of bovine albumin in nonaqueous media. Arch. Biochem. Biophys. 50, 515–517 (1954)

    Google Scholar 

  • Lewis, P.N., Scheraga, H.A.: Predictions of structural homologies in cytochrome c proteins. Arch. Biochem. Biophys. 144, 576–583 (1971)

    Google Scholar 

  • Lingrel, J.B., Webster, G.: Serum-albumin synthesis by isolated rat liver microsomes. Biochem. Biophys. Res. Commun. 5, 57–62 (1961)

    Google Scholar 

  • Lloyd, E.A., Saunders, S.J., Frith, L.O.C., Wright, J.E.: Albumin synthesis and catabolism following partial hepatectomy in the rat. The effects of amino acids and adrenocortical steroids on albumin synthesis after partial hepatectomy. Biochim. Biophys. Acta 402, 113–123 (1975)

    Google Scholar 

  • Lodish, H.F.: Biosynthesis of reticulocyte membrane proteins by membrane-free polyribosomes. Proc. Natl. Acad. Sci. USA 70, 1526–1530 (1973)

    Google Scholar 

  • Lodish, H.F.: Translational control of protein synthesis. Annu. Rev. Biochem. 45, 39–72 (1976)

    Google Scholar 

  • Lucas-Lenard, J., Lipman, F.: Protein biosynthesis. Annu. Rev. Biochem. 40, 409–448 (1971)

    Google Scholar 

  • Madden, S.C., Whipple, G.H.: Plasma proteins: their source, production and utilization. Physiol. Rev. 20, 194–217 (1940)

    Google Scholar 

  • Maeno, H., Schreiber, G., Weigand, K., Weinssen, U., Zhringer, J.: Impairment of albumin synthesis in cell-free systems from rat liver. FEBS Lett. 6, 137–140 (1970)

    Google Scholar 

  • Malawista, S.E., Weiss, M.C.: Expression of differentiated functions in hepatoma cell hybrids: high frequency of induction of mouse albumin production in rat hepatoma-mouse lymphoblasts hybrids. Proc. Natl. Acad. Sci. USA 71, 927–931 (1974)

    Google Scholar 

  • Mancini, G., Carbonara, A.O., Heremans, J.F.: Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry 2, 235–254 (1965)

    Google Scholar 

  • Mans, R.J., Novelli, G.D.: A convenient, rapid and sensitive method for measuring the incorporation of radioactive amino acids into protein. Biochem. Biophys. Res. Commun. 3, 540–543 (1960)

    Google Scholar 

  • Mans, R.J., Novelli, G.D.: Measurement of the incorporation of radioactive amino acids into protein by a filter-paper disk method. Arch. Biochem. Biophys. 94, 48–53 (1961)

    Google Scholar 

  • Margulies, M.M.: Concerning the sites of synthesis of proteins of chloroplast ribosomes and of fraction I protein (ribulose-l,5-diphosphate carboxylase). Biochem. Biophys. Res. Commun. 44, 539–545 (1971)

    Google Scholar 

  • Marsh, J.B., Drabkin, D.L.: Metabolic channeling in experimental nephrosis. IV. Net synthesis of plasma albumin by liver slices from normal and nephrotic rats. J. Biol. Chem. 230, 1073–1081 (1958)

    Google Scholar 

  • Marsh, J.B., Drabkin, D.L.: Experimental reconstruction of metabolic pattern of lipid nephrosis: key role of hepatic protein synthesis in hyperlipemia. Metabolism 9, 946–955 (1960)

    Google Scholar 

  • Marsh, J.B., Drabkin, D.L.: Stimulation of plasma albumin synthesis by rat-liver ribo-nucleic acid. Biochim. Biophys. Acta 95, 173–176 (1965)

    Google Scholar 

  • Marsh, J.B., Drabkin, D.L., Braun, G.A., Parks, J.S.: Factors in the stimulation of protein synthesis by subcellular preparations from rat liver. J. Biol. Chem. 241, 4168–4174 (1966)

    Google Scholar 

  • Maurer, R.A., Gorski, J., McKean, D.J.: Partial amino acid sequence of rat pre-prolactin. Biochem. J. 161, 189–192 (1977)

    Google Scholar 

  • May, B.K., Elliott, W.H.: Characteristics of extracellular protease formation by Bacillus subtilis and its control by amino acid repression. Biochim. Biophys. Acta 157, 607–615 (1968)

    Google Scholar 

  • McGown, E., Richardson, A.G., Henderson, L.M., Swan, P.B.: Effect of amino acids on ribosome aggregation and protein synthesis in perfused liver. J. Nutr. 103, 109–116 (1973)

    Google Scholar 

  • McLaughlin, C.A., Pitot, H.C.: The effect of various treatments in vitro and in vivo on the binding of 125I-labelled anti-rat serum albumin Fab' to rat tissue polyribosomes. Biochemistry 15, 3541–3550 (1976)

    Google Scholar 

  • McMenamy, R.H.: Association of indole analogues to defatted human serum albumin. Arch. Biochem. Biophys. 103, 409–417 (1963)

    Google Scholar 

  • McMenamy, R.H.: Binding of indole analogues to human serum albumin. J. Biol. Chem. 240, 4235–4243 (1965)

    Google Scholar 

  • McMenamy, R.H., Oncley, J.L.: The specific binding of L-tryptophan to serum albumin. J. Biol. Chem. 233, 1436–1447 (1958)

    Google Scholar 

  • Michael, S.E.: The isolation of albumin from blood serum or plasma by means of organic solvents. Biochem. J. 82, 212–218 (1962)

    Google Scholar 

  • Miller, L.L., Bly, C.G., Bale, W.F.: Plasma and tissue proteins produced by non-hepatic rat organs as studied with lysine-ε-C14. J. Exp. Med. 99, 133–153 (1954)

    Google Scholar 

  • Miller, L.L., Bly, C.G., Watson, M.L., Bale, W.F.: The dominant role of the liver in plasma protein synthesis. A direct study of the isolated perfused rat liver with the aid of lysine-ε-C 14. J. Exp. Med. 94, 431–453 (1951)

    Google Scholar 

  • Millership, A.S.: Synthesis and secretion of bovine serum albumin. M. Sc. Thesis, University of Melbourne, 1977.

    Google Scholar 

  • Millership, A., Schreiber, G., Christie, B.: Synthesis and secretion of bovine serum albumin. Proc. Aust. Biochem. Soc. 10, 56 (1977)

    Google Scholar 

  • Milstein, C, Brownlee, G.G., Harrison, T.M., Mathews, M.B.: A possible precursor of immunoglobulin light chains. Nature (Lond.) 239, 117–120 (1972)

    Google Scholar 

  • Moon, K.E., Thompson, E.O.P.: Subunits from reduced and S-carboxymethylated ribulose diphosphate carboxylase (fraction I protein). Aust. J. Biol. Sci. 22, 463–470 (1969)

    Google Scholar 

  • Morgan, E.H.: Transferrin and albumin distribution and turnover in the rat. Am. J. Physiol. 211, 1486–1494 (1966)

    Google Scholar 

  • Morgan, E.H., Peters, T., Jr.: The biosynthesis of rat serum albumin. V. Effect of protein depletion and refeeding on albumin and transferrin synthesis. J. Biol. Chem. 246, 3500–3507 (1971a)

    Google Scholar 

  • Morgan, E.H., Peters, T., Jr.: Intracellular aspects of transferrin synthesis and secretion in the rat. J. Biol. Chem. 246, 3508–3511 (1971b)

    Google Scholar 

  • Morgenthaler, J.-J., Mendiola-Morgenthaler, L.: Synthesis of soluble, thylakoid, and envelope membrane proteins by spinach chloroplasts purified from gradients. Arch. Biochem. Biophys. 172, 51–58 (1976)

    Google Scholar 

  • Mullins, F., Weissman, S.M., Konen, J.A.: Extraabdominal serum protein synthesis in the rhesus monkey. J. Surg. Res. 6, 315–321 (1966)

    Google Scholar 

  • Munro, H.N.: A general survey of mechanisms regulating protein metabolism in mammals. In: Mammalian Protein Metabolism. Munro, H.N. (ed.), Vol. IV, pp. 3–130. New York—London: Academic Press 1970

    Google Scholar 

  • Mycek, M.J., Clarke, D.D., Neidle, A., Waelsch, H.: Amine incorporation into insulin as catalyzed by transglutaminase. Arch. Biochem. Biophys. 84, 528–540 (1959)

    Google Scholar 

  • Nardacci, N.J., Jones, J.P., Hall, A.L., Olson, R.E.: Synthesis of nascent prothrombin and albumin in a heterologous system using rat liver messenger RNA purified on oligo (dT)-cellulose. Biochem. Biophys. Res. Commun. 64, 51–58 (1975)

    Google Scholar 

  • Neidle, A., Mycek, M.J., Clarke, D.D., Waelsch, H.: Enzymic exchange of protein amide groups. Arch. Biochem. Biophys. 77, 227–229 (1958)

    Google Scholar 

  • Ogata, K.: Protein biosynthesis-translation: albumin biosynthesis. Igakunoaumi 58, 344–350 (1966)

    Google Scholar 

  • Ogata, K.: Biosynthesis of serum albumin. Tampakushitsu Kakusan Koso 12, 1346–1351 (1967)

    Google Scholar 

  • Ogata, K.: Serum albumin biosynthesis. Taisya 10, 281–290 (1973)

    Google Scholar 

  • Ogata, K., Hirokawa, R., Omori, S.: Incorporation of leucine into microsomal albumin by microsomes and pH-5 enzymes from normal rat liver. Biochim. Biophys. Acta 40, 178–179 (1960)

    Google Scholar 

  • Ogata, K., Ishikawa, K., Tominaga, H., Watanabe, I., Morita, T., Sugano, H.: Further evidence for the existence of a specific ribonucleic acid in liver ribosomes. Biochim. Biophys. Acta 76, 630–632 (1963)

    Google Scholar 

  • Ogata, K., Omori, S., Hirokawa, R., Takahashi, T.: Studies of the Cell Free System for Biosynthesis of Serum Albumin in Liver Cells and Serum γ-Globulin in Immune Spleen Cells. Proc. 5th Int. Congr. Biochem. Moscow, Symp. 2, pp. 183–194, 1961

    Google Scholar 

  • Ohanian, S.H., Taubman, S.B., Thorbecke, G.J.: Rates of albumin and transferrin synthesis in vitro in rat hepatoma-derived H4II-EC3 cells. J. Natl. Cancer Inst. 43, 397–406 (1969)

    Google Scholar 

  • Oler, A., Lombardi, B.: Further studies on a defect in the intracellular transport and secretion of proteins by the liver of choline-deficient rats. J. Biol. Chem. 245, 1282–1288 (1970)

    Google Scholar 

  • Otten, J., Jonckheer, M., Dumont, J.E.: Thyroid albumin. II. In vitro synthesis of a thyroid albumin by normal human thyroid tissue. J. Clin. Endocrinol. Metab. 32, 18–26 (1971)

    Google Scholar 

  • Ove, P., Coetzee, M.L., Chen, J., Morris, H.P.: Differences in synthesis and degradation of serum proteins in normal and hepatoma-bearing animals. Cancer Res. 32, 2510–2518 (1972)

    Google Scholar 

  • Pain, R.H., Robson, B.: Analysis of the code relating sequence to secondary structure in proteins. Nature (Lond.) 227, 62–63 (1970)

    Google Scholar 

  • Papaconstantinou, J., Ledford, B.E.: Regulation of albumin synthesis in cultured mouse hepatoma cells. In: The Role of RNA in Reproduction and Development. Niu, M.C., Segal, S.J. (eds.), pp. 43–52. Amsterdam: North-Holland 1973

    Google Scholar 

  • Patterson, J.E., Geller, D.M.: Bovine microsomal albumin: amino terminal sequence of bovine proalbumin. Biochem. Biophys. Res. Commun. 74, 1220–1226 (1977)

    Google Scholar 

  • Peters, T., Jr.: A serum albumin precursor in cytoplasmic particles. J. Biol. Chem. 229, 659–677 (1957)

    Google Scholar 

  • Peters, T., Jr.: The isolation of serum albumin from specific precipitates of serum albumin and its rabbit antibodies. J. Am. Chem. Soc. 80, 2700–2702 (1958)

    Google Scholar 

  • Peters, T., Jr.: Cytoplasmic particles and serum albumin synthesis. J. Histochem. Cyto-chem. 7, 224–234 (1959)

    Google Scholar 

  • Peters, T., Jr.: The biosynthesis of rat serum albumin. I. Properties of rat albumin and its occurrence in liver cell fractions. J. Biol. Chem. 237, 1181–1185 (1962a)

    Google Scholar 

  • Peters, T., Jr.: The biosynthesis of albumin. II. Intracellular phenomena in the secretion of newly formed albumin. J. Biol. Chem. 237, 1186–1189 (1962b)

    Google Scholar 

  • Peters, T., Jr.: Serum albumin. Adv. Clin. Chem. 13, 37–111 (1970)

    Google Scholar 

  • Peters, T., Jr.: Serum albumin. In: The Plasma Proteins. Structure, Function and Genetic Control. Putman, F.W. (ed.), 2nd ed., Vol. I, pp. 133–181. New York—San Francisco—London: Academic Press 1975.

    Google Scholar 

  • Peters, T., Jr.: Serum albumin: recent progress in the understanding of its structure and biosynthesis. Clin. Chem. 23, 5–12 (1977)

    Google Scholar 

  • Peters, T., Jr., Anfinsen, C.B.: Production of radioactive serum albumin by liver slices. J. Biol. Chem. 182, 171–179 (1950a)

    Google Scholar 

  • Peters, T., Jr., Anfinsen, C.B.: Net production of serum albumin by liver slices. J. Biol. Chem. 186, 805–813 (1950b)

    Google Scholar 

  • Peters, T., Jr., Danzi, J.T., Ashley, C.A.: Effect of the rate of albumin synthesis on the proportion of hepatocytes containing demonstrable serum albumin. Fed. Proc. 27, 775 (1968)

    Google Scholar 

  • Peters, T., Jr., Fleischer, B., Fleischer, S.: The biosynthesis of rat serum albumin. IV. Apparent passage of albumin through the Golgi apparatus during secretion. J. Biol. Chem. 246, 240–244 (1971)

    Google Scholar 

  • Peters, T., Jr., Peters, J.C.: The biosynthesis of rat serum albumin. VI. Intracellular transport of albumin and rates of albumin and liver protein synthesis in vivo under various physiological conditions. J. Biol. Chem. 247, 3858–3863 (1972)

    Google Scholar 

  • Peterson, J.A.: Assay for albumin-messenger-RNA in an in vitro protein synthesizing system from wheat germ. Nucl. Acids Res. 3, 1427–1436 (1976)

    Google Scholar 

  • Peterson, J.A., Weiss, M.C.: Expression of differentiated functions in hepatoma cell hybrids: induction of mouse albumin production in rat hepatoma-mouse fibroblast hybrids. Proc. Natl. Acad. Sci. USA 69, 571–575 (1972)

    Google Scholar 

  • Putnam, F.W.: Thyroxine-binding prealbumin. In: The Plasma Proteins. Structure, Function and Genetic. Control. Putman, F.W. (ed.), 2nd ed., Vol. I, pp. 70–72. New York—San Francisco—London: Academic Press 1975

    Google Scholar 

  • Quinn, P.S., Gamble, M., Judah, J.D.: Biosynthesis of serum albumin in rat liver. Isolation and probable structure of ‘proalbumin’ from rat liver. Biochem. J. 146, 389–393 (1975)

    Google Scholar 

  • Race, J.: The determination of blood-proteins by acid-acetone. Biochem. J. 26, 1571–1584 (1932)

    Google Scholar 

  • Rao, K.R., Tarver, H.: Albumin synthesis and release-stimulation with fat rich super-natants and differences between free and bound ribosomes of normal and regenerating rat livers. Fed. Proc. 29, 919 (1970)

    Google Scholar 

  • Redman, C.M.: The synthesis of serum proteins on attached rather than free ribosomes of rat liver. Biochem. Biophys. Res. Commun. 31, 845–850 (1968)

    Google Scholar 

  • Redman, C.M.: Biosynthesis of serum proteins and ferritin by free and attached ribosomes of rat liver. J. Biol. Chem. 244, 4308–4315 (1969)

    Google Scholar 

  • Redman, CM., Banerjee, D., Howell, K., Palade, G.E.: Colchicine inhibition of plasma protein release from rat hepatocytes. J. Cell Biol. 66, 42–59 (1975)

    Google Scholar 

  • Redman, CM., Cherian, M.G.: The secretory pathways of rat serum glycoproteins and albumin: localization of newly formed proteins within the endoplasmic reticulum. J. Cell Biol. 52, 231–245 (1972)

    Google Scholar 

  • Redman, C.M., Grab, D.J., Irukulla, R.: The intracellular pathway of newly formed rat liver catalase. Arch. Biochem. Biophys. 152, 496–501 (1972)

    Google Scholar 

  • Richardson, U.I., Tashjian, A.H., Jr., Levine, L.: Establishment of a clonal strain of hepatoma cells which secrete albumin. J. Cell. Biol. 40, 236–247 (1969)

    Google Scholar 

  • Roberts, B.E., Paterson, B.M., Sperling, R.: The cell-free synthesis and assembly of viral specific polypeptides into TMV particles. Virology 59, 307–313 (1974)

    Google Scholar 

  • Rossing, N.: The normal metabolism of 131I-labelled albumin in man. Clin. Sci. 33, 593–602 (1967)

    Google Scholar 

  • Rotermund, H.-M., Schreiber, G., Maeno, H., Weinssen, U., Weigand, K.: The ratio of albumin synthesis to total protein synthesis in normal rat liver, in host liver, and in Morris hepatoma 9121. Cancer Res. 30, 2139–2146 (1970)

    Google Scholar 

  • Rothschild, M.A., Oratz, M., Mongelli, J., Schreiber, S.S.: Effects of a short-term fast on albumin synthesis studied in vivo, in the perfused liver, and on amino acid incorporation by hepatic microsomes. J. Clin. Invest. 47, 2591–2599 (1968)

    Google Scholar 

  • Rothschild, M.A., Oratz, M., Mongelli, J., Schreiber, S.S.: Effect of albumin concentration on albumin synthesis in the perfused liver. Am. J. Physiol. 216, 1127–1130 (1969)

    Google Scholar 

  • Rothschild, M.A., Oratz, M., Schreiber, S.S.: Current concepts of albumin metabolism, a review. Gastroenterology 58, 402–408 (1970)

    Google Scholar 

  • Rothschild, M.A., Oratz, M., Schreiber, S.S.; Albumin synthesis. (First of two parts). N. Engl. J. Med. 286, 748–757 (1972a)

    Google Scholar 

  • Rothschild, M.A., Oratz, M., Schreiber, S.S.: Albumin synthesis. (Second of two parts). N. Engl. J. Med. 286, 816–820 (1972b)

    Google Scholar 

  • Rothschild, M.A., Oratz, M., Schreiber, S.S.: Albumin metabolism. Gastroenterology 64, 324–337 (1973)

    Google Scholar 

  • Rothschild, M.A., Oratz, M., Schreiber, S.S.: Regulation of albumin metabolism. Annu. Rev. Med. 26, 91–104 (1975)

    Google Scholar 

  • Rothschild, M.A., Oratz, M., Wimer, E., Schreiber, S.S.: Studies on albumin synthesis: The effects of dextran and cortisone on albumin metabolism in rabbits studied with albumin-I131. J. Clin. Invest. 40, 545–554 (1961)

    Google Scholar 

  • Roy, H., Patterson, R., Jagendorf, A.T.: Identification of the small subunit of ribulose 1,5-bisphosphate carboxylase as a product of wheat leaf cytoplasmic ribosomes. Arch. Biochem. Biophys. 172, 64–73 (1976)

    Google Scholar 

  • Russell, J.H., Geller, D.M.: Rat serum albumin biosynthesis: evidence for a precursor. Biochem. Biophys. Res. Commun. 55, 239–245 (1973)

    Google Scholar 

  • Russell, J.H., Geller, D.M.: The structure of rat proalbumin. J. Biol. Chem. 250, 3409–3413 (1975)

    Google Scholar 

  • Rutner, A.C., Lane, M.D.: Nonidentical subunits of ribulose diphosphate carboxylase. Biochem. Biophys. Res. Commun. 28, 531–537 (1967)

    Google Scholar 

  • Samarina, O.P., Zbarskii, I.B., Perevoshchikova, K.A.: The binding of labeled amino acids by protein and nucleic acid preparations. Biokhimiia 25, 443–451 (1960)

    Google Scholar 

  • Sandor, G.: Serum Proteins in Health and Disease. London: Chapman and Hall Ltd. 1966

    Google Scholar 

  • Sandor, G., Sureau, B., Martin, L., Berrod, J., Martin, R.: Hépatite virale et l'origine de l'albumine sé rique. C.R. Acad. Sci. (D) (Paris) 265, 1560–1563 (1967)

    Google Scholar 

  • Sargent, J.R., Campbell, P.N.: The sequential synthesis of the polypeptide chain of serum albumin by the microsome fraction of rat liver. Biochem. J. 96, 134–146 (1965)

    Google Scholar 

  • Sarkar, N.K., Clarke, D.D., Waelsch, H.: An enzymatically catalyzed incorporation of amines into proteins. Biochim. Biophys. Acta 25, 451–452 (1957)

    Google Scholar 

  • Sarner, N.Z., Bissell, M.J., DiGirolamo, M., Gorini, L.: Mechanism of excretion of a bacterial proteinase: demonstration of two proteolytic enzymes produced by a Sarcina strain (Coccus P). J. Bacteriol. 105, 1090–1098 (1971)

    Google Scholar 

  • Schechter, I., Burstein, Y.: Partial sequence of the precursors of immunoglobulin light-chains of different subgroups: evidence that the immunoglobulin variable-region gene is larger than hitherto known. Biochem. Biophys. Res. Commun. 68, 489–496 (1976a)

    Google Scholar 

  • Schechter, I., Burstein, Y.: Marked hydrophobicity of the NH2-terminal extra piece of immunoglobulin light-chain precursors: possible physiological functions of the extra piece. Proc. Natl. Acad. Sci. USA 73, 3273–3277 (1976b)

    Google Scholar 

  • Schechter, I., Burstein, Y.: Identification of N-terminal methionine in the precursor of immunoglobulin light chain. Intitiation of translation of messenger ribonucleic acid in plants and animals. Biochem. J. 153, 543–550 (1976c)

    Google Scholar 

  • Schreiber, G.: Studien zur Sekretion und Synthese von Serumalbumin in normaler, regenerierender und maligne entarteter Rattenleber. Habilitationsschrift, Freiburg, 1970

    Google Scholar 

  • Schreiber, G.: Translation of genetic information on the ribosome. Angew. Chemie (Engl.) 10, 638–651 (1971)

    Google Scholar 

  • Schreiber, G.: Applications of radioactively labelled antigen-antibody complexes in biochemistry. In: Radioactive Tracers in Microbial Immunology. Kaufmann, B. (ed.), pp. 49–54. Vienna: International Atomic Energy Agency 1972

    Google Scholar 

  • Schreiber, G., Boutwell, R.K., Potter, V.R., Morris, H.P.: Lack of secretion of serum protein by transplanted rat hepatomas. Cancer Res. 26, 2357–2361 (1966)

    Google Scholar 

  • Schreiber, G., Edwards, K., Schreiber, M.: Energy dependence of protein synthesis and secretion in cell suspensions from rat liver. Proc. Aust. Biochem. Soc. 10, 34 (1977a)

    Google Scholar 

  • Schreiber, G., Lesch, R., Weinssen, U., Zähringer, J.: The distribution of albumin synthesis throughout the liver lobule. J. Cell Biol. 47, 285–289 (1970)

    Google Scholar 

  • Schreiber, G., Rotermund, H.-M., Maeno, H., Weigand, K., Lesch, R.: The proportion of the incorporation of leucine into albumin to that into total protein in rat liver and hepatoma Morris 5123TC. Eur. J. Biochem. 10, 355–361 (1969)

    Google Scholar 

  • Schreiber, G., Schreiber, M.: The preparation of single cell suspensions from liver and their use for the study of protein synthesis (Review). Sub-Cell Biochem. 2, 307–353 (1973)

    Google Scholar 

  • Schreiber, G., Schreiber, M.: Protein synthesis and excretion in single cell suspensions from liver and Morris hepatoma 5123TC. In: Gene Expression and Carcinogenesis in Cultured Liver. Gerschenson, L.E., Thompson, E.G. (eds.), pp. 46–61. New York-San Francisco-London: Academic Press 1975

    Google Scholar 

  • Schreiber, G., Urban, J., Dryburgh, H., Bradley, T.R.: The synthesis and secretion of serum albumin in Morris hepatomas 5123TC and 9121. In: Morris Hepatomas: Mechanisms of Regulation. Morris, H.P., Criss, W.E. (eds.). New York: Adv. in Exp. Med. Biol., Plenum Publishing Corp. 1977b (in press)

    Google Scholar 

  • Schreiber, G., Urban, J., Edwards, K.: Possible functions of the oligopeptide extension in the albumin precursor. J. Theor. Biol. 60, 241–245 (1976a)

    Google Scholar 

  • Schreiber, G., Urban, J., Edwards, K., Dryburgh, H., Inglis, A.S.: Mechanism and regulation of albumin synthesis in liver and hepatomas. Adv. Enzyme Regul. 14, 163–184 (1976b)

    Google Scholar 

  • Schreiber, G., Urban, J., Zähringer, J., Reutter, W., Frosch, U.: The secretion of serum protein and the synthesis of albumin and total protein in regenerating rat liver. J. Biol. Chem. 246, 4531–4538 (1971)

    Google Scholar 

  • Schreiber, M., Schreiber, G., Kartenbeck, J.: Protein and ribonucleic acid metabolism in single-cell suspensions from Morris hepatoma 5123TC and from normal rat liver. Cancer Res. 34, 2143–2150 (1974)

    Google Scholar 

  • Schultze, H.E., Heremans, J.F.: Nature and metabolism of extracellular proteins. In: Molecular Biology of Human Proteins, Vol. I. Amsterdam—London—New York: Elsevier 1966

    Google Scholar 

  • Schwert, G.W.: Recovery of native bovine serum albumin after precipitation with tri-chloroacetic acid and solution in organic solvents. J. Am. Chem. Soc. 79, 139–141 (1957)

    Google Scholar 

  • Segrest, J.P., Jackson, R.L., Marchesi, V.T., Guyer, R.B., Terry, W.: Red cell membrane glycoprotein: amino acid sequence of an intramembranous region. Biochem. Biophys. Res. Commun. 49, 964–969 (1972)

    Google Scholar 

  • Segrest, J.P., Kahane, I., Jackson, R.L., Marchesi, V.T.: Major glycoprotein for the human erythrocyte membrane: evidence for an amphipathic molecular structure. Arch. Biochem. Biophys. 155, 167–183 (1973)

    Google Scholar 

  • Shafritz, D.A.: Protein synthesis with messenger ribonucleic acid fractions from membrane-bound and free liver polysomes. Translation characteristics of liver polysomal ribonucleic acids and evidence for albumin production in a messenger-dependent reticulocyte cell-free system. J. Biol. Chem. 249, 81–88 (1974)

    Google Scholar 

  • Shapiro, D.J., Taylor, J.M., McKnight, G.S., Palacios, R., Gonzalez, C, Kiely, M.L., Schimke, R.T.: Isolation of hen oviduct ovalbumin and rat liver albumin polysomes by indirect immunoprecipitation. J. Biol. Chem. 249, 3665–3671 (1974)

    Google Scholar 

  • Shore, G.C., Tata, J.R.: Two fractions of rough endoplasmic reticulum from rat liver. II. Cytoplasmic messenger RNA's which code for albumin and mitochondrial proteins are distributed differently between the two fractions. J. Cell Biol. 72, 726–743 (1977)

    Google Scholar 

  • Smallwood, R.A., Jones, E.A., Craigie, A., Raia, S., Rosenoer, V.M.: The delivery of newly synthesized albumin and fibrinogen to the plasma in dogs. Clin. Sci. 35, 35–43 (1968)

    Google Scholar 

  • Soffer, R.L.: The arginine transfer reaction. Biochim. Biophys. Acta 155, 228–240 (1968)

    Google Scholar 

  • Soffer, R.L.: Enzymatic modification of proteins. II. Purification and properties of the arginyl transfer ribonucleic acid-protein transferase from rabbit liver cytoplasm. J. Biol. Chem. 245, 731–737 (1970)

    Google Scholar 

  • Soffer, R.L.: Enzymatic modification of proteins. V. Protein acceptor specificity in the arginine-transfer reaction. J. Biol. Chem. 246, 1602–1606 (1971)

    Google Scholar 

  • Soffer, R.L.: Peptide acceptors in the leucine, phenylalanine transfer reaction. J. Biol. Chem. 248, 8424–8428 (1973)

    Google Scholar 

  • Soffer, R.L., Horinishi, H.: Enzymatic modifications of proteins. I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm. J. Mol. Biol. 43, 163–175 (1969)

    Google Scholar 

  • Soffer, R.L., Horinishi, H., Leibowitz, M.J.: The aminoacyl tRNA-protein transferases. Cold Spring Harbor Symp. Quant. Biol. 34, 529–533 (1969)

    Google Scholar 

  • Soffer, R.L., Mendelsohn, N.: Incorporation of arginine by a soluble system from sheep thyroid. Biochem. Biophys. Res. Commun. 23, 252–258 (1966)

    Google Scholar 

  • Sonenshein, G.E, Brawerman, G.: Differential translation of rat liver albumin messenger RNA in a wheat germ cell-free system. Biochemistry 16, 5445–5448 (1977)

    Google Scholar 

  • Spatz, L., Strittmatter, P.: A form of cytochrome b 5 that contains an additional hydrophobic sequence of 40 amino acid residues. Proc. Natl. Acad. Sci. USA 68, 1042–1046 (1971)

    Google Scholar 

  • Spector, A.A.: Fatty acid binding to plasma albumin (Review). J. Lipid Res. 16, 165–179 (1975)

    Google Scholar 

  • Steiner, D.F., Cunningham, D., Spigelman, L., Aten, B.: Insulin biosynthesis: evidence for a precursor. Science 157, 697–700 (1967)

    Google Scholar 

  • Steiner, D.F., Kemmler, W., Tager, H.S., Peterson, J.D.: Proteolytic processing in the biosynthesis of insulin and other proteins. Fed. Proc. 33, 2105–2115 (1974)

    Google Scholar 

  • Steiner, R.F., Roth, J., Robbins, J.: The binding of thyroxine by serum albumin as measured by fluorescence quenching. J. Biol. Chem. 241, 560–567 (1966)

    Google Scholar 

  • Sterling, K.: Molecular structure of thyroxine in relation to its binding by human serum albumin. J. Clin. Invest. 43, 1721–1729 (1964)

    Google Scholar 

  • Sterling, K., Rosen, P., Tabachnik, M.: Equilibrium dialysis studies of the binding of thyroxine by human serum albumins. J. Clin. Invest. 41, 1021–1030 (1962)

    Google Scholar 

  • Sterling, K., Tabachnick, M.: Determination of the binding constants for the interaction of thyroxine and its analogues with human serum albumin. J. Biol. Chem. 236, 2241–2243 (1961)

    Google Scholar 

  • Stewart, K.K., Doherty, R.F.: Resolution of DL-tryptophan by affinity chromato-graphy on bovine-serum albumin-agarose columns. Proc. Natl. Acad. Sci. USA 70, 2850–2852 (1973)

    Google Scholar 

  • Strauss, A.W., Bennett, C.D., Donohue, A.M., Rodkey, J.A., Alberts, A.W.: Rat liver preproalbumin: Complete amino acid sequence of the pre-piece. J. Biol. Chem. 252, 6846–6855 (1977)

    Google Scholar 

  • Strauss, A.W., Donohue, A.M., Bennett, C.D., Rodkey, J.A., Alberts, A.W.: Rat liver preproalbumin: in vitro synthesis and partial amino acid sequence. Proc. Natl. Acad. Sci. USA 74, 1358–1362 (1977b)

    Google Scholar 

  • Suchanek, G., Kindas-Mügge, I., Kreil, G., Schreier, M.H.: Translation of honeybee promelittin messenger RNA. Formation of a larger product in a mammalian cell-free system. Eur. J. Biochem. 60, 309–315 (1975)

    Google Scholar 

  • Szentivanyi, A., Radovich, J., Talmage, D.W.: The separation of free, disulphide-bound and peptide-bound S 35 radioactivity in serum and tissues. J. Infect. Dis. 109, 231–237 (1961)

    Google Scholar 

  • Tabachnick, M.: Thyroxine-protein interactions. I. Binding of thyroxine to human serum albumin and modified albumins. J. Biol. Chem. 239, 1242–1249 (1964)

    Google Scholar 

  • Tager, H.S., Steiner, D.F.: Isolation of a glucagon-containing peptide: primary structure of a possible fragment of proglucagon. Proc. Natl. Acad. Sci. USA 70, 2321–2325 (1973)

    Google Scholar 

  • Takagi, M., Ogata, K.: Direct evidence for albumin biosynthesis by membrane bound polysomes in rat liver. Biochem. Biophys. Res. Commun. 33, 55–60 (1968)

    Google Scholar 

  • Takagi, M., Ogata, K.: Isolation of serum albumin-synthesizing polysomes from rat liver. Biochem. Biophys. Res. Commun. 42, 125–131 (1971)

    Google Scholar 

  • Takagi, M., Tanaka, T., Ogata, K.: Evidence for exclusive biosynthesis in vivo of serum albumin by bound polysomes of rat liver. J. Biochem. (Tokyo) 65, 651–653 (1969)

    Google Scholar 

  • Takagi, M., Tanaka, T., Ogata, K.: Functional differences in protein synthesis between free and bound polysomes of rat liver. Biochim. Biophys. Acta 217, 148–158 (1970)

    Google Scholar 

  • Takanami, M.: Labelling of microsomal proteins with radioactive amino acids. Biochim. Biophys. Acta 37, 556–557 (1960)

    Google Scholar 

  • Takeda, Y., Reeve, E.B.: Studies of the metabolism and distribution of albumin with autologous I131-albumin in healthy men. J. Lab. Clin. Med. 61, 183–202 (1963)

    Google Scholar 

  • Tanaka, Y., Kaji, H.: Incorporation of arginine by soluble extracts of ascites tumor cells and regenerating rat liver. Cancer Res. 34, 2204–2208 (1974)

    Google Scholar 

  • Tanaka, S., Scheraga, H.A.: Statistical mechanical treatment of protein conformation. 4. A four-state model for specific-sequence copolymers of amino acids. Macromole-cules 9, 812–833 (1976)

    Google Scholar 

  • Tarver, H., Reinhardt, W.O.: Methionine labeled with radioactive sulfur as an indicator of protein formation in the hepatectomized dog. J. Biol. Chem. 167, 395–400 (1947)

    Google Scholar 

  • Tashjian, A.H., Jr., Bancroft, F.C., Richardson, U.I., Goldlust, M.B., Rommel, F.A.. Ofner, P.: Multiple differentiated functions in an unusual clonal strain of hepatoma cells. In Vitro 6, 32–45 (1970)

    Google Scholar 

  • Tavill, A.S., Nadkarni, D., Metcalfe, J., Black, E., Hoffenberg, R., Carson, E.R.: Hepatic albumin and urea synthesis. The mathematical modelling of the dynamics of [14C] carbonate-derived guanidine-labelled arginine in the isolated perfused rat liver. Biochem. J. 150, 495–509 (1975)

    Google Scholar 

  • Taylor, J.M., Schimke, R.T.: Synthesis of rat liver albumin in a rabbit reticulocyte cell-free protein-synthesizing system. J. Biol. Chem. 248, 7661–7668 (1973)

    Google Scholar 

  • Taylor, J.M., Tse, T.P.H.: Isolation of rat liver albumin messenger RNA. J. Biol. Chem. 251, 7461–7467 (1976)

    Google Scholar 

  • Thibodeau, S.N., Gagnon, J., Palmiter, R.: Precursor forms of lysozyme and ovomucoid: sequence analysis. Fed. Proc. 36, 656 (1977)

    Google Scholar 

  • Tracht, M.E., Tallal, L., Tracht, D.G.: Intrinsic hepatic control of plasma albumin concentration. Life Sci. 6, 2621–2628 (1967)

    Google Scholar 

  • Tritsch, G.L., Rathke, C.E., Tritsch, N.E., Weiss, C.M.: Thyroxine binding by human serum albumin. J. Biol. Chem. 236, 3163–3167 (1961)

    Google Scholar 

  • Tse, T.P.H., Taylor, J.M.: Translation of albumin messenger RNA in a cell-free protein-synthesizing system derived from wheat germ. J. Biol. Chem. 252, 1272–1278 (1977)

    Google Scholar 

  • Urban, J., Chelladurai, M., Millership, A., Schreiber, G.: The kinetics in vivo of the synthesis of albumin-like protein and albumin in rats. Eur. J. Biochem. 67, 477–485 (1976)

    Google Scholar 

  • Urban, J., Inglis, A.S., Edwards, K., Schreiber, G.: Chemical evidence for the difference between albumins from microsomes and serum and a possible precursor-product relationship. Biochem. Biophys. Res. Commun. 61, 494–501 (1974a)

    Google Scholar 

  • Urban, J., Kartenbeck, J., Zimber, P., Timko, J., Lesch, R., Schreiber, G.: Increase of extravascular albumin pool and the intracellular accumulation of vesicles in transplanted Morris hepatoma 9121. Cancer Res. 32, 1971–1977 (1972)

    Google Scholar 

  • Urban, J., Schreiber, G.: Biological evidence for a precursor protein of serum albumin. Biochem. Biophys. Res. Commun. 64, 778–782 (1975)

    Google Scholar 

  • Urban, J., Zimber, P., Schreiber, G.: Immunoprecipitation is inappropriate for the isolation of radiochemically pure albumin from tissues. Anal. Biochem. 58, 102–116 (1974b)

    Google Scholar 

  • Verkleij, A.J., Zwaal, R.F.A., Roelofsen, B., Comfurius, P., Kastelijn, D., van Deenen, L.L.M.: The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy. Biochim. Biophys. Acta 323, 178–193 (1973)

    Google Scholar 

  • Volkin, E., Cohn, W.E.: Estimation of nucleic acids. In: Methods of Biochemical Analysis. Glick, D. (ed.), Vol. I, pp. 287–305. New York: Interscience 1954

    Google Scholar 

  • Wachsmuth, E.D., Jost, J.-P.: Localization of vitellogenin and serum albumin in hepatic parenchymal cells of normal and estradiol-treated immature chickens. Biochim. Biophys. Acta 437, 454–461 (1976)

    Google Scholar 

  • Wasserman, K., Joseph, J.D., Mayerson, H.S.: Kinetics of vascular and extravascular protein exchange in unbled and bled dogs. Am. J. Physiol. 184, 175–182 (1956)

    Google Scholar 

  • Waterlow, J.C.: The assessment of protein nutrition and metabolism in the whole animal, with special reference to man. In: Mammalian Protein Metabolism. Munro, H.N. (ed.), Vol. III, pp. 325–390. New York—London: Academic Press 1969

    Google Scholar 

  • Weigand, K.: Die Regulation des Serumalbuminspiegels unter physiologischen und pathologischen Bedingungen. Klin. Wschr. 55, 295–305 (1977a)

    Google Scholar 

  • Weigand, K.: Serumprotein-Synthese in isolierten Leberzellen. Fortschr. Med. 95, 1272–1276 (1977b)

    Google Scholar 

  • Weigand, K., Müller, M., Urban, J., Schreiber, G.: Intact endoplasmic reticulum and albumin synthesis in rat liver cell suspensions. Exp. Cell Res. 67, 27–32 (1971)

    Google Scholar 

  • Weigand, K., Otto, I.: Secretion of serum albumin by enzymatically isolated rat liver cells. FEBS Lett. 46, 127–129 (1974)

    Google Scholar 

  • Williams, C.A., Ganoza, M.C., Lipmann, F.: Effect of bacterial infection on the synthesis of serum proteins by a mouse liver cell-free system. Proc. Natl. Acad. Sci. USA 53, 622–626 (1965)

    Google Scholar 

  • Wise, R.W., Ballard, F.J., Ezekiel, E.: Developmental changes in the plasma protein pattern of the rat. Comp. Biochem. Physiol. 9, 23–30 (1963)

    Google Scholar 

  • Wise, R.W., Oliver, I.T.: Sites of synthesis of plasma proteins in the foetal rat. Biochem. J. 100, 330–333 (1966)

    Google Scholar 

  • Yanagida, M.: Isolation by affinity chromatography of a precursor head protein (P23) of bacteriophage T4. J. Mol. Biol. 87, 317–327 (1974)

    Google Scholar 

  • Yu, S., Redman, C: In vitro synthesis of rat pre-proalbumin. Biochem. Biophys. Res. Commun. 76, 469–476 (1977)

    Google Scholar 

  • Zähringer, J., Baliga, B.S., Drake, R.L., Munro, H.N.: Distribution of ferritin mRNA and albumin mRNA between free and membrane-bound rat liver polysomes. Biochim. Biophys. Acta 474, 234–244 (1977)

    Google Scholar 

  • Zhringer, J., Baliga, B.S., Munro, H.N.: Increased levels of microsomal albumin-mRNA in the liver of nephrotic rats. FEBS Lett. 62, 322–325 (1976)

    Google Scholar 

  • Zilversmit, D.B., Entenman, C, Fishier, M.C.: On the calculation of “turnover time” and “turnover rate” from experiments involving the use of labeling agents. J. Gen. Physiol. 26, 325–331 (1943)

    Google Scholar 

  • Zimmon, D.S., Oratz, M., Kessler, R., Schreiber, S.S., Rothschild, M.A.: Albumin to ascites: demonstration of a direct pathway bypassing the systemic circulation. J. Clin. Invest. 48, 2074–2078 (1969)

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

Copyright information

© 1978 Springer-Verlag

About this chapter

Cite this chapter

Schreiber, G., Urban, J. (1978). The synthesis and secretion of albumin. In: Reviews of Physiology, Biochemistry and Pharmacology, Volume 82. Reviews of Physiology, Biochemistry and Pharmacology, vol 82. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0030497

Download citation

  • DOI: https://doi.org/10.1007/BFb0030497

  • Published:

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-08748-9

  • Online ISBN: 978-3-540-35883-1

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics