Acta physiologica latino americana 1980-01-01

The kininases of Bothrops jararaca plasma.

A A Lavras, M Fichman, E Hiraichi, T Tobo, M A Boucault

Index: Acta Physiol. Lat. Am. 30(4) , 269-74, (1980)

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Abstract

Evidence is presented to suggest that kininase activity of Bothrops jararaca plasma is due to the presence of at least three distinct enzymes: a carboxypeptidase B type enzyme, similar to that found in human plasma in that its activity is enhanced by Co2+ (1 X 10(-4) M); a carboxypeptidase B type enzyme whose activity is unaffected by Co2+, and an enzyme which cleaves bradykinin to liberate Phe-Arg as the major peptide fragment formed. The latter enzyme is responsible for the major kininase activity of this snake plasma and is identified as a dipeptide hydrolase.

Related Compounds

  • Hippuryl-Lys-OH

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