TY - JOUR
T1 - Affinity labelling of carboxypeptidase B
T2 - Modification of a methionyl residue
AU - Zisapel, Nava
AU - Sokolovsky, Mordechai
PY - 1974/6/18
Y1 - 1974/6/18
N2 - Modification of porcine carboxypeptidase B with [14C]-bromoacetyl-p-aminobenzylsuccinic acid results in a marked decrease of the activity toward both peptide and ester substrates. The inactivation correlates with the incorporation of 1 equivalent of inhibitor molecule per carboxypeptidase molecule. Evidence is presented that inactivation is due to alkylation of a single, presumably methionyl residue in the active center of the enzyme.
AB - Modification of porcine carboxypeptidase B with [14C]-bromoacetyl-p-aminobenzylsuccinic acid results in a marked decrease of the activity toward both peptide and ester substrates. The inactivation correlates with the incorporation of 1 equivalent of inhibitor molecule per carboxypeptidase molecule. Evidence is presented that inactivation is due to alkylation of a single, presumably methionyl residue in the active center of the enzyme.
UR - http://www.scopus.com/inward/record.url?scp=0016164466&partnerID=8YFLogxK
U2 - 10.1016/S0006-291X(74)80236-6
DO - 10.1016/S0006-291X(74)80236-6
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AN - SCOPUS:0016164466
SN - 0006-291X
VL - 58
SP - 951
EP - 959
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -