Hostname: page-component-cd9895bd7-8ctnn Total loading time: 0 Render date: 2024-12-31T19:10:04.798Z Has data issue: false hasContentIssue false
  • English
  • Français

A rennin-sensitive bond in αs1 Β-casein

Published online by Cambridge University Press:  01 June 2009

R. D. Hill ,
E. Lahav  and
D. Givol
R. D. Hill
Affiliation:
Dairy Research Laboratory, Division of Food Research, C.S.I.R.O., Highett, Victoria, Australia
E. Lahav
Affiliation:
Volcani Institute of Agricultural Research, Rehovot, Israel
D. Givol
Affiliation:
Department of Immunochemistry, Weizmann Institute of Science, Rehovot, Israel
Get access Rights & Permissions [Opens in a new window]

Summary

Rennin acts on a specially sensitive bond in αs1 B-casein to produce a basic peptide containing residues 1–23 of the original protein. At pH 6·4 and 30°C, the action is specific and rapid, the kinetic constants being Km 4·5×10−4M, Kcat 3·8 s−1, and kcat/Km 0·85×104 s−1 M−1. Pepsin, and a protease impurity in the acid phosphatase from wheat germ, have a similar action.

Type
Research Article
Information
Journal of Dairy Research , Volume 41 , Issue 1 , February 1974 , pp. 147 - 153
Copyright
Copyright © Proprietors of Journal of Dairy Research 1974

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Beeby, R. (1970). Biochimica et Biophysica Acta 214, 364.CrossRefGoogle Scholar
Brignon, G., Mercier, J-C. & Ribadeau-Dumas, B. (1972). FEBS Letters 27, 301.CrossRefGoogle Scholar
Berridge, N. J. (1952). Analyst 77, 57.CrossRefGoogle Scholar
Creamer, L. K., Mills, O. E. & Richards, E. L. (1971). Journal of Dairy Research 38, 269.CrossRefGoogle Scholar
El Negoumy, A. M. (1970). Journal of Dairy Research 37, 437.CrossRefGoogle Scholar
Fish, J. C. (1957). Nature 180, 345.CrossRefGoogle Scholar
Fox, P. F. (1969). Journal of Dairy Research 36, 427.CrossRefGoogle Scholar
Garnier, J. (1963). Biochimica et Biophysica Acta 66, 366.CrossRefGoogle Scholar
Hill, R. D. (1963). Journal of Dairy Research 30, 101.CrossRefGoogle Scholar
Hill, R. D. (1968). Biochemical and Biophysical Research Communications 33, 659.CrossRefGoogle Scholar
Hill, R. D. (1969). Journal of Dairy Research 36, 409.CrossRefGoogle Scholar
Hill, R. D. & Laing, R. (1967). Biochimica et Biophysica Acta 132, 188.CrossRefGoogle Scholar
Hipp, N. J., Groves, M. L., Custer, J. H. & McMeekin, T. L. (1952). Journal of Dairy Science 35, 272.CrossRefGoogle Scholar
Lahav, E. & Babad, Y. (1964). Journal of Dairy Research 31, 31.CrossRefGoogle Scholar
Lindqvist, B. & Storgårds, T. (1960). Acta Chemica Scandinavica 14, 757.CrossRefGoogle Scholar
Lineweaver, H. & Burk, D. (1934). Journal of the American Chemical Society 56, 658.CrossRefGoogle Scholar
McPherson, H. T. (1946). Biochemical Journal 40, 470.CrossRefGoogle Scholar
Mercier, J. C., Grosclaude, F. & Ribadeau-Dumas, B. (1971). European Journal of Biochemistry 23, 41.CrossRefGoogle Scholar
Polzhofer, K. P. (1972). Tetrahedron 28, 855.CrossRefGoogle Scholar
Raymond, M. N., Garnier, J., Bricas, E., Cilianu, S., Blasnic, M., Chaix, A. & Lefrancier, P. (1972). Biochimie 54, 145.CrossRefGoogle Scholar
Sachdev, G. P., Johnston, M. A. & Fruton, J. S. (1972). Biochemistry 11, 1080.CrossRefGoogle Scholar
Schattenkerk, C., Holtkamp, I., Hessing, J. G. M., Kerling, K. E. T. & Havinga, E. (1971). Recueil des Travaux Chimiques des Pays-Bas 90, 1320.CrossRefGoogle Scholar
Tam, J. J. & Whitaker, J. R. (1972). Journal of Dairy Science 55, 1523.CrossRefGoogle Scholar
Zittle, C. A. & Custer, J. H. (1963). Journal of Dairy Science 46, 1183.CrossRefGoogle Scholar