Summary
The effect of specific ligands (the substrate glucose 1-phosphate, AMP, and flavins) on the initial rate of tryptic digestion of muscle glycogen phosphorylase b has been studied (0.02 M HEPES, pH 6.8; 37°C). Differences were observed between the kinetic curves of the enzyme trypsinolysis initiated by the addition of a trypsin/ligand mixture and once trypsin was added to the enzyme preincubated with a ligand for 10 min. It was suggested that the specific ligands studied induce relatively slow conformational changes in the phosphorylase b molecule.
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References
Barford, D., and Johnson, L.N. (1989) The allosteric transition of glycogen phosphorylase. Nature 340: 609 – 616.
Johnson, L.N., Hajdu, J., Acharya, K.R., Stuart, D.I., McLaughlin, P.L., Oikonomakos, N.G., and Barford, D. (1989) Glycogen phosphorylase h. In: Herve, G. (ed.): Allosteric Enzymes, CRC Press, Boca Raton, pp. 81 – 127.
Fisher, E.H., and Krebs, E.G. (1962) Muscle phosphorylase b. In: Kaplan, N.O. (ed.): Methods in Enzymology, vol. 5, Academic Press, New York, pp. 369 – 373.
Kureanov, B.I., Lissovskaya, N.P., and Livanova, N.B. (1972) On the spatial distinction of ligand-binding sites in phosphorylase h. Biokhimiya 37: 289–298 (In Russian).
Marshall, M., and Fahien, L.A. (1988) Proteolysis as a probe of ligand-associated conformational changes in rat carbonyl phosphate synthetase 1. Arch. Biochem. Biophys. 262: 455–470.
Smith, A.D., and Wilson. J.E. (1991) Effect of ligand binding on the tryptic digestion pattern of rat brain hexokinase: relationship of ligand-induced conformational changes to catalytic and regulatory functions. Arch. Biochem. Biophys. 291: 59 – 68.
Kurganov, B.I., Schors, E.I., Livanova, N.B., Chebotareva, N.A., Eronina, T.B., Andreeva, I.E., Makeeva, V.Ph., and Pekel', N.D. (1993) Effect of flavins on the rate of proteolytic digestion of muscle glycogen phosphorylase b. Biochimie 75: 481 – 485.
Kurganov, B.I. (1982) Allosteric Enzymes. Kinetic Behaviour. John Wiley & Sons, Chichester, 344 pp.
Frieden, C. (1970) Kinetic aspects of regulation of metabolic processes. The hysteretic enzyme concept. J. Biol. Chem. 245: 5788 – 5799.
Frieden, C. (1979) Slow transitions and hysteretic behavior in enzymes. Annu. Rev. Biochem. 48: 471 – 489.
Neet, K.E., and Ainslie, G.R. (1980) Hysteretic enzymes. In: Purich, D.L. (ed.): Methods in Enzymology, vol. 64, Enzyme Kinetics and Mechanisms, Part B, Academic Press, New York, pp. 192 – 226.
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© 1994 Birkhäuser Verlag Basel/Switzerland
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Kurganov, B.I., Schors, E.I. (1994). Slow conformational transitions of muscle glycogen phosphorylase b . In: Marino, G., Sannia, G., Bossa, F. (eds) Biochemistry of Vitamin B6 and PQQ. Advances in Life Sciences. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-7393-2_28
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DOI: https://doi.org/10.1007/978-3-0348-7393-2_28
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