AI Article Synopsis
- The study examined the peptide-hydrolyzing action of a highly purified kininase enzyme from the venom of the Latrodectus Tredecimguttatus spider using thin-layer chromatography (TLC) with synthetic peptides as substrates.
- The enzyme was found to specifically cleave the -Pro(7)-Phe(8)-bonds in bradykinin (BK) and angiotensin I (AI), releasing respective C-terminal dipeptide and tripeptide products.
- The results indicate that kininase acts as a thiol endopeptidase, targeting internal peptide bonds near the proline carboxyl end, with no exopeptidase activity observed on various tri- and pentapeptides.
Article Abstract
The specificity of the peptide hydrolyzing action of a highly purified preparation of kininase from Latrodectus Tredecimguttatus venom was studied by the method of TLC on silica gel with the use of various synthetic peptides as substrates. It was shown that the enzyme cleaves the -Pro(7)-Phe(8)-bonds in BK and AI molecules liberating, correspondingly, the C-terminal dipeptide and tripeptide. Exopeptidase specificity was not revealed in the enzyme activity with the use of a number of free and N-substituted tri- and pentapeptides. The results obtained characterize the spider venom kininase as a thiol endopeptidase, which cleaves internal peptide bonds at the proline carboxyl end.
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Kininase of the Latrodectus tredecimguttatus venom: a study of its enzyme substrate specificity.
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Article Synopsis
- The study examined the peptide-hydrolyzing action of a highly purified kininase enzyme from the venom of the Latrodectus Tredecimguttatus spider using thin-layer chromatography (TLC) with synthetic peptides as substrates.
- The enzyme was found to specifically cleave the -Pro(7)-Phe(8)-bonds in bradykinin (BK) and angiotensin I (AI), releasing respective C-terminal dipeptide and tripeptide products.
- The results indicate that kininase acts as a thiol endopeptidase, targeting internal peptide bonds near the proline carboxyl end, with no exopeptidase activity observed on various tri- and pentapeptides.
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For the first time by method of gel-filtration and ionexchange chromatography two bradykinin-potentiating peptides have been isolated in homogeneous state from Latrodectus tredecimguttatus spider venom. The homogeneity was proved by disk-electrophoresis, isoelectrical focusing, analysis of aminoacid content and rechromatography. Peptides are acid proteins with molecular mass 10,000 and 2500 D.
View Article and Find Full Text PDFThe nature of the bradykinin (BK)-hydrolyzing (kininase) activity of peptidhydrolase isolated from spider (Latr. tredecimguttatus) venom has been studied. It was found that the BKase activity of the enzyme is fully inhibited by organic mercurials (10(-5)-10(-6) M) as well as by 5,5'-dithiobis(2-nitrobenzoic acid) (10(-7) M); the latter blocks three SH-groups within the enzyme molecule.
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