Trapeznikova S S, Gontar' I D
Vopr Med Khim. 1977 Nov-Dec(6):840-4.
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.
羧肽酶N与溴化氰活化的琼脂糖凝胶4B共价结合，酶活性未降低。固定化酶与人血浆中的天然低分子抑制剂相互作用时，会形成稳定的钴离子依赖性复合物，该复合物在2M氯化钠存在下会部分解离。所得数据表明，所研究的抑制剂对羧肽酶N活性具有特异性作用。
