MAJOR KININASES IN RAT URINE ARE NEUTRAL ENDOPEPTIDASE AND CARBOXYPEPTIDASE Y-LIKE EXOPEPTIDASE

摘要: Two types of kininases were separated from rat urine by gel-filtration on a column Superdex 200 and characterized as membrane-bound neutral endopeptidase (EC 3.4.24.11) carboxypeptidase Y-like exopeptidase. The which was found in void volume fraction, liberated first Phe 8 -Arg 9 then 5 -Ser 6 -Pro 7 bradykinin (BK) * . kininase activity inhibited phosphoramidon thiorphan but not captopril. Another with an apparent molecular weight 93,000 cleaved rapidly BK into BK1-8 (des Arg BK) BK1-7 BK1-6 Pro -Phe