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Synthetic peptide and ester substrates for rennin

Published online by Cambridge University Press:  01 June 2009

R. D. Hill
R. D. Hill
Affiliation:
Division of Dairy Research, C.S.I.R.O., Melbourne, Australia
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Summary

Rennin hydrolysed the phe-met bond in the peptide H-ser-leu-phe-met-ala-OMe (i.e. methyl ester), the amino acid sequence of which is similar to that around the phe-met bond attacked by rennin in κ-casein. Rennin did not attack other peptides from this sequence not containing serine, and it is suggested that, in both κ-casein and the pentapeptide, the enzymic attack is accelerated by the nearby serine side chain. Rennin also hydrolysed sulphite esters such as phenyl sulphite ester and some N-substituted imidazole compounds such as benzoyl imidazole. Phenyl sulphite esters may be suitable substrate for assaying the activity of preparations of rennin.

Type
Original Articles
Information
Journal of Dairy Research , Volume 36 , Issue 3 , October 1969 , pp. 409 - 415
Copyright
Copyright © Proprietors of Journal of Dairy Research 1969

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