Skip to main content
SpringerLink
Log in

Properties of placental alkaline phosphatase. III. Thermostability and urea inhibition of isolated components of the three common phenotypes

  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

Different heat inactivation rates were found among the three common homozygous human placental alkaline phosphatase phenotypes with respect to component I (the rapidly migrating component). Phenotype I1 was less stable than F1 and S1, while types F1 and S1 exhibited very similar thermostabilities, F1 being slightly more stable than S1. Components I, IIα (the fastest of the slow-moving components), and IIβ (the group of the very slowly migrating components) had different heat stabilities, IIβ being the most stable and I the least stable. Magnesium greatly increased the heat stability of all tested phenotypes. Placental alkaline phosphatase was found to be less heat resistant than reported previously. All phenotypes were equally inhibited over urea concentrations ranging from 0.5 to 8 m. No difference in the inhibition rate was found among components I, IIα, IIβ, and the crude placental butanol extract. The altered electrophoretic pattern of the crude placental extract obtained by urea starch gel electrophoresis was considered as being most likely due to reversible changes in the folding of the molecules.

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

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Bahr, M., and Wilkinson, J. H. (1967). Urea as a selective inhibitor of human tissue alkaline phosphatases. Clin. Chim. Acta 17 367.

    Google Scholar 

  • Beckman, G. (1970). Placental alkaline phosphatase, relation between phenotype and enzyme activity. Human Hered. 20 74.

    Google Scholar 

  • Beratis, N. G., Seegers, W., and Hirschhorn, K. (1970). Properties of placental alkaline phosphatase. I. Molecular size and electrical charge of the various electrophoretic components of the six common phenotypes. Biochem. Genet. 4 689.

    Google Scholar 

  • Beratis, N. G., Seegers, W., and Hirschhorn, K. (1971). Properties of placental alkaline phosphatase. II. Interactions of fast- and slow-migrating components. Biochem. Genet. 5 367.

    Google Scholar 

  • Birkett, D. J., Conyers, R. A. J., Neale, F. C., Posen, S., and Brudenell-Woods, J. (1967). Action of urea on human alkaline phosphatases: With a description of some automated techniques for the study of enzyme kinetics. Arch. Biochem. Biophys. 121 470.

    Google Scholar 

  • Boyer, S. H. (1961). Alkaline phosphatase in human sera and placentae. Science 134 1002.

    Google Scholar 

  • Boyer, S. H. (1963). Human organ alkaline phosphatases: Discrimination by several means including starch gel electrophoresis of antienzyme-enzyme supernatant fluids. Ann. N. Y. Acad. Sci. 103 938.

    Google Scholar 

  • Butterworth, P. J., and Moss, D. W. (1966). The effect of urea on human kidney alkaline phosphatase. Biochem. J. 99: 9P.

    Google Scholar 

  • Fishman, W. H., Inglis, N. R., Green, S., Anstiss, C. L., Gosh, N. K., Reif, A. E., Rustigian, R., Krant, M. J., and Stolbach, L. L. (1968). Immunology and biochemistry of Regan isoenzyme of alkaline phosphatase in human cancer. Nature 219 697.

    Google Scholar 

  • Morgenstern, S., Kessler, G., Auerbach, J., Flor, R., and Klein, B. (1965). An automated p-nitrophenylphosphate procedure for the AutoAnalyzer. Clin. Chem. 11 876.

    Google Scholar 

  • Morton, R. K. (1954). The purification of alkaline phosphatases of animal tissues. Biochem. J. 57 595.

    Google Scholar 

  • Neale, F. C., Clubb, J. S., Hotchkis, D., and Posen, S. (1965). Heat stability of human placental alkaline phosphatase. J. Clin. Pathol. 18 359.

    Google Scholar 

  • Poulik, M. D. (1957). Starch gel electrophoresis in a discontinuous system of buffers. Nature 180 1477.

    Google Scholar 

  • Poulik, M. D. (1963). Electrophoretic map of chemically derived sub-units of papain-digested γ-globulin. Nature 198 752.

    Google Scholar 

  • Poulik, M. D. (1964). Starch gel immunoelectrophoresis. Ann. N. Y. Acad. Sci. 121 470.

    Google Scholar 

  • Robson, E. B., and Harris, H. (1965). Genetics of the alkaline phosphatase polymorphism of the human placenta. Nature 207 1257.

    Google Scholar 

  • Robson, E. B., and Harris, H. (1967). Further studies on the genetics of placental alkaline phosphatase. Ann. Human Genet. 30 219.

    Google Scholar 

  • Smithies, O, Connell, G. E., and Dixon, G. H. (1962). Inheritance of haptoglobin subtypes. Am. J. Human Genet. 14 14.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Division of Medical Genetics, Department of Pediatrics, Mount Sinai School of Medicine of the City University of New York, New York, New York

    Nicholas G. Beratis & Kurt Hirschhorn (Career Scientist of the Health Research Council of the City of New York (I-513)

Authors
  1. Nicholas G. Beratis
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Kurt Hirschhorn
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

This work was supported in part by U.S. Public Health Service Grant HDO2552.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Beratis, N.G., Hirschhorn, K. Properties of placental alkaline phosphatase. III. Thermostability and urea inhibition of isolated components of the three common phenotypes. Biochem Genet 6, 1–8 (1972). https://doi.org/10.1007/BF00485959

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00485959

Keywords

Search

Navigation