This preclinical study demonstrates the presence of inactive, trypsin-activated renin in dog plasma and kidney renin granules, with a much higher ratio of inactive to active renin in plasma compared to stored renin.
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Higher plasma inactive-to-active renin ratio than in granules in dogs; leaves open its role in human renin-angiotensin regulation.
Trypsin-activated renin (inactive renin) was detected in the break-through fraction when dog plasma or renin extracted from renin granules (stored renin) was applied to a pepstatin column, respectively. The appearance of the renin activity by trypsin treatment was not due to acid protease. Production of angiotensin I from homologous renin substrate by the trypsin-activated renin was proportional to the time of incubation. The trypsin-activated renin had an affinity for the pepstatin column. The maximum amount of trypsin-activated renin was obtained with incubation for 15 min at 37 degrees C at 1000 micrograms/ml in plasma or at 100 micrograms/ml in case of stored renin. The ratio of inactive to active renin was calculated to be 1.6 or 0.002 in plasma or stored renin, respectively, under conditions of a standard sodium diet.
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Kawamura et al. (1983) studied this question.
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