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  • Title: [Trypsin and microbial serine proteinase inhibitors isolated from Yersinia pseudotuberculosis].
    Author: Burftseva TI, Kofanova NN.
    Journal: Biokhimiia; 1996 Oct; 61(10):1883-91. PubMed ID: 9011235.
    Abstract:
    A novel 9 kD protein inhibitor of trypsin and related proteinases was purified from culture filtrate of Yersinia pseudotuberculosis by ultrafiltration, affinity chromatography, and gel filtration. The protein is stable at pH from 1 to 9. The inhibitor activity dramatically decreases at temperature above 37 degrees C. The purified inhibitor significantly suppresses activities of an endogenous trypsin-related proteinase and trypsin but does not affect chymotrypsin, pepsin, and papain. One molecule of yersinia inhibitor binds two molecules of endogenous trypsin-related proteinase and about one trypsin molecule. The Ki for yersinia proteinase is 1.7.10(-7) and Ki for trypsin is 2.4.10(-7). Amino acid composition of the inhibitor is characterized by the presence of beta-aminobutyric acid and ornithine and relatively high contents of alanine and arginine whereas cysteine, histidine, and proline are absent.
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