TY - JOUR
T1 - Basic and Non‐Basic Substrates of Carboxypeptidase B
AU - Zisapel, Nava
AU - Kurn‐Abramowitz, Nurith
AU - Sokolovsky, Mordechai
PY - 1973/6
Y1 - 1973/6
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0015783429&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1973.tb02866.x
DO - 10.1111/j.1432-1033.1973.tb02866.x
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AN - SCOPUS:0015783429
SN - 0014-2956
VL - 35
SP - 507
EP - 511
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 3
ER -