The kininases of Bothrops jararaca plasma
Lavras, A.A.; Fichman, M.; Hiraichi, E.; Tobo, T.; Boucault, M.A.
Acta Physiologica Latino Americana 30(4): 269-274
1980
ISSN/ISBN: 0001-6764 PMID: 6100945 Document Number: 161366
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.