The Chromatographic and kinetic properties of acid- and pepsin-activated inactive renin from human amniotic fluid were determined. Acid-activated inactive renin, like inactive renin, was found to be bound to an Affi-Gel Blue affinity column. Pepsin-activated inactive renin, on the other hand, did not bind to such a column. The Km values of endogenous active renin, acid-activated inactive renin, and pepsin-activated inactive renin with bovine substrate were 0.11, 0.12 and 0.05 μM respectively. With hog substrate, the Km values were 0.16,0.19 and 0.10 μM respectively. These results suggest that there is a difference between the active form of renin obtained from acid activation of inactive renin and the active renin obtained after pepsin treatment.
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