Asunto(s)
Presión Sanguínea/efectos de los fármacos , Venenos de Crotálidos/farmacología , Serpientes/sangre , Tripsina/farmacología , Animales , Bradiquinina/farmacología , Columbidae , Ácido Elágico/farmacología , Femenino , Técnicas In Vitro , Masculino , Contracción Muscular/efectos de los fármacos , Músculo Liso/efectos de los fármacos , Peptidil-Dipeptidasa A/sangre , Ratas , Contracción Uterina/efectos de los fármacosRESUMEN
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.
Asunto(s)
Carboxipeptidasas/sangre , Serpientes/sangre , Sulfato de Amonio/farmacología , Animales , Bradiquinina/metabolismo , Carboxipeptidasa B , Carboxipeptidasas/aislamiento & purificación , Precipitación Química , Pruebas Enzimáticas Clínicas , Cobalto/farmacología , Hidrólisis , Lisina/análogos & derivados , Lisina/metabolismo , Peptidil-Dipeptidasa A/aislamiento & purificaciónRESUMEN
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.
RESUMEN
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.
