The effective use of affinity chromatography for the study of complex formation of bovine carboxypeptidase B with basic and aromatic amino acid analogues

Abstract

The affinity chromatography method was applied to the study of the binding of carboxypeptidase B to basic and aromatic amino acid analogues. This method revealed that these two kinds of ligands occupy different sites on the enzyme and the affinity of its binding site(s) for aromatic substrates or inhibitors was profoundly influenced by the occupation of the other site(s) by ϵ-aminocaproic acid.