Feb 1, 1976

Isolation and several properties of Streptomyces griseus carboxypeptidase

Biokhimii︠a︡
A S TsyperovichT F Kastrikina

Abstract

Enzymatic and physico-chemical properties of homogenous preparation of carboxypeptidase from Streptomyces griseus are studied. pH-Optimum is found to be 7.9 and 8.2 under the hydrolysis of cbs-Gly-Leu and hyppuryl-arg respectively, temperature optimum --60 degrees C. The enzyme splits more efficiently basic amino acids and leucine from N-terminal-protected dipeptides. Str. griseus carboxypeptidase is activated by reducting agents (NaCN, cisteine, ascorbic acid), it is inhibited by KMnO4 and it does not belong to "serine" type enzymes. SH-groups are essential for the enzyme activity. No significant effect of metal ions on the enzyme activity is observed. The inhibitory effect of EDTA developed only after the prolonged treatment. The enzyme has one N-terminal group (alanine), which evidences the presence of one polypeptide chain in the enzyme molecule.

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Mentioned in this Paper

Enzymes, antithrombotic
Amino Acids, I.V. solution additive
Ascorbic Acid Measurement
Enzyme Activity
Enzymes for Treatment of Wounds and Ulcers
Blood Enzyme Activity (Lab Test)
Catalysis
Carboxypeptidase [EPC]
Carboxypeptidase
Serine

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