Citation

Akhunov AA, Makevnina LG, Golubenko Z, Paskhina TS. Immunopharmacology 1996; 32(1-3): 160-162.

Affiliation

Institute of Bioorganic Chemistry, Academy of Sciences, Uzbekistan, Russia.

Copyright

(Copyright © 1996, Elsevier Publishing)

DOI

unavailable

PMID

8796297

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.

Language: en