Abstract
It was demonstrated that angiotensin I-converting enzyme was excreted in human urine. The mean activity of the enzyme in normal urine was found to be 0.38 ± 0.04 (S.E.M.) units/day ( n = 18) and the enzymic activity correlated well with the concentration of the excreted sodium ( r = 0.76, p < 0.005). Urinary angiotensin I-converting enzyme was partially purified. Three different molecular weights of enzyme (>400 000, 290 000 and 140 000) were demonstrated by Sephadex G-200 gel filtration. The enzymic properties of these three enzymes were identical with those of angiotensin I-converting enzyme from human lung with regard to inhibitory effects (bradykinin potentiator c and Arg-Pro-Pro), Cl −3 dependency, pH optimum and K m value.
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