By-product analogs for bovine carboxypeptidase B

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Abstract
A series of monocarboxylic and dicarboxylic acid S-containing by-product analogues of lysine and arginine was synthesized and tested as competitive inhibitors of bovine carboxypeptidase B. The most effective derivatives were guanidinoethylmercaptosuccinic acid and aminopropylmercaptosuccinic acid with Ki [inhibitor binding constant] of 4 and 8 .times. 10-6 M, respectively. Kinetic studies established the pure competitive nature of the inhibition. Mixed studies with the alkylating reagents bromoacetyl-D-arginine and bromoacetamidobutylguanidine established their efficiency in protecting the active-center glutamic acid and tyrosine of bovine carboxypeptidase B, respectively, from irreversible alkylation. Kinetic studies with bovine carboxypeptidase A and porcine carboxypeptidase B showed a lack of efficiency for A and high degree of efficiency for B.