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Comparative Study
. 1997 Feb;62(2):171-5.

Purification and characterization of serine proteinase of the Glu,Asp-specific enzyme family from Thermoactinomyces species

I V Demidyuk  1 , E A Nosovskaya, I A Tsaplina, G I Karavaiko, S V Kostrov
Affiliations
  • PMID: 9159871
Comparative Study

Purification and characterization of serine proteinase of the Glu,Asp-specific enzyme family from Thermoactinomyces species

I V Demidyuk et al. Biochemistry (Mosc). 1997 Feb.

Abstract

Enzyme catalyzing hydrolysis of a substrate of Glu,Asp-specific proteinases (Z-Glu-pNA) and cleaving bond Glu13-Ala14 in the oxidized insulin B chain was purified to homogeneity from the culture medium of Thermoactinomyces species using hydrophobic chromatography on phenyl-Sepharose CL 4B as the key purification step. The molecular weight of the proteinase is 23 kD. The enzyme is completely inhibited by diisopropyl fluorophosphate and is stable at pH 5-11. The pH optimum for the hydrolysis of azocasein as substrate is 8.5. The temperature optimum for proteolytic activity is 55 degrees C. The N-terminal sequence of the proteinase is: Ser-Val-Leu-Gly-Thr-Asp-Glu-Arg-Thr-Arg-Val-Thr-Asn-Thr-Thr-Thr-Tyr-Pro- Tyr- Trp-.

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