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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
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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

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