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  • Title: Purification and characterization of serine proteinase of the Glu,Asp-specific enzyme family from Thermoactinomyces species.
    Author: Demidyuk IV, Nosovskaya EA, Tsaplina IA, Karavaiko GI, Kostrov SV.
    Journal: Biochemistry (Mosc); 1997 Feb; 62(2):171-5. PubMed ID: 9159871.
    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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