Human urinary angiotensin I-converting enzyme was partially purified by DEAF-cellulose and Sephadex G-200 chromatography. The molecular weight of the enzyme was estimated to be 400, 000, 290, 000 and 40, 000 by Sephadex G-200 gel filtration. These isozymes however showed the same optimal pH (8.3) and temperature (37°), and a similar sensitivity towards various inhibitors. The urinary excretion of converting enzyme was 244.6±227.0 (mean±S.D.) units/day in 31 patients with essential hypertension, 380±177.3 units/day in 5 patients with chronic glomerulonephritis, 324.0 units/day in a patient with renovascular hypertension, 288.5 units/day in a patient with primary aldosteronism, and 229.6±73.9 units/day in 5 normal subjects. There was a significant positive correlation between the enzyme excretion and sodium excretion in hypertensive patients (r=0.701, p<0.001), but no significant relationships were observedd among the excretion of the enzyme, creatinine and potassium, and the plasma renin activity (PRA) and aldosterone concentration (PAC). The urinary converting enzyme was increased by f urosemide and upright posture, significantly correlated with the excreted sodium, but not with the potassium and creatinine excretion, PRA and PAC in hypertensive patients as well as in normal subjects. The urinary angiotensin I-converting enzyme, which may derive from the kidney, plays a possible role in the regulation of sodium excretion in cooperation with the renal kallikreinkinin system in hypertensive patients.
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