[Interaction of immobilized carboxypeptidase with a natural inhibitor from human blood plasma].
Carboxypeptidase N was bound covalently to CNBr-activated Sepharose 4B without decrease in the enzymatic activity. Interaction of the immobilized enzyme with native low molecular inhibitor from human blood plasma was accompanied by formation of the stable Co2+-dependent complex, which is partially dissociated in presence of 2 M NaCl. The data obtained suggest that the inhibitor studied possesses the specific effect on the carboxypeptidase N activity.
D002268:Carboxypeptidases / Q000037:antagonists & inhibitors*; D004791:Enzyme Inhibitors / Q000097:blood*; D004800:Enzymes, Immobilized; D006801:Humans; D066298:In Vitro Techniques; D001121:Lysine Carboxypeptidase / Q000037:antagonists & inhibitors*
D004791:Enzyme Inhibitors; D004800:Enzymes, Immobilized; D002268:Carboxypeptidases; D001121:Lysine Carboxypeptidase
Vzaimodeĭstvie immobilizovannoĭ karboksipeptidazy s prirodnym ingibitorom iz plazmy krovi cheloveka.