Open AccessBasic and Non‐Basic Substrates of Carboxypeptidase B
Author(s) -
Zisapel Nava,
KurnAbramowitz Nurith,
Sokolovsky Mordechai
Publication year - 1973
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1973.tb02866.x
Subject(s) - carboxypeptidase , carboxypeptidase a , hydrolysis , chemistry , kinetics , amino acid , stereochemistry , biochemistry , enzyme , physics , quantum mechanics
The kinetics of porcine‐carboxypeptidase‐B‐catalyzed hydrolysis of several N‐blocked peptides that differ in size and in C‐terminal amino acid were examined. The data demonstrate different kinetic behaviour of carboxypeptidase‐B‐catalyzed hydrolysis of basic and non‐basic substrates. These studies are consistent with our proposed multiple loci model. The results also show a number of differences between carboxypeptidases A and B, as well as several similarities.