title: The kininases of Bothrops jararaca plasma.
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.
mesh_terms: D000645:Ammonium Sulfate / Q000494:pharmacology; D000818:Animals; D001920:Bradykinin / Q000378:metabolism; D043424:Carboxypeptidase B; D002268:Carboxypeptidases / Q000097:blood* / Q000302:isolation & purification; D011232:Chemical Precipitation; D004796:Clinical Enzyme Tests; D003035:Cobalt / Q000494:pharmacology; D006868:Hydrolysis; D008239:Lysine / Q000031:analogs & derivatives / Q000378:metabolism; D007703:Peptidyl-Dipeptidase A / Q000302:isolation & purification; D012911:Snakes / Q000097:blood*
chemical_list: D003035:Cobalt; C007945:hippuryl-L-lysine; D002268:Carboxypeptidases; D007703:Peptidyl-Dipeptidase A; D043424:Carboxypeptidase B; D008239:Lysine; D001920:Bradykinin; D000645:Ammonium Sulfate