Application of Carboxypeptidase Cu to Amino Acid Sequence Analysis. I. Preparation and Enzymatic Properties of Immobilized Carboxypeptidase C_Ua

抄録

Carboxypeptidase C_Ua, isolated from the exocarp of Citrus unshiu MARC., was bound to CNBr-activated agarose with coupling yields of 74-99%. The immobilized enzyme possessed 77-122% of the activity of the native enzyme and was stable to repeated assays and prolonged storage. It showed a broad substrate specificity similar to that of the native enzyme and liberated amino acids including proline sequentially from the C-termini of angiotensin I, bradykinin potentiator C, the oxidized B chain of bovine insulin, and bovine plasma albumin.