M. Hajjou et al., PURIFICATION AND SOME PROPERTIES OF A CARBOXYPEPTIDASE-B FROM DOGFISHSCYLIORHINUS-CANICULA, Comparative biochemistry and physiology. B. Comparative biochemistry, 110(4), 1995, pp. 791-798
A carboxypeptidase B (CPB) has been purified from dogfish (Scyliovhinu
s canicula) pancreas and partially characterized, The purification pro
cedure included acetone precipitation, ion-exchange chromatography on
a CM-cellulose column and gel filtration on Sephadex G-75, The purifie
d enzyme migrates as a single band both on PAGE and SDS-PAGE, Its mole
cular mass is estimated to be about 32 kDa. The optimum of activity is
obtained at pH 7.5-8.2. The enzyme is inhibited by typical metal-chel
ating agents (EDTA and o-phenanthroline) and by Hg2+, It is activated
by Co2+, L-cysteine and by heat treatment at 40 degrees and 50 degrees
C, Kinetic parameters, K-m and k(cat), of native enzyme, Co2+-activat
ed CPB and heat-treated CPB have been determined.