This preclinical study demonstrates the existence of two distinct types of inactive renin: a zymogen form and a stable renin-inhibitor complex.
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Animal data on inactive renin forms should not change practice; leaves open translation to human cardiovascular disease.
To determine the molecular properties of inactive renin and its relationship to active renin, inactive renin in hog kidney was purified by devising affinity chromatography. Electrophoretically homogeneous inactive renin was prepared by 3 million-fold purification. It consists of a single polypeptide chain and undergoes reduction in molecular weight from 50,000 to 38,000 upon activation by proteases but not by dissociative treatment. This type of inactive renin is considered as a zymogen. However, a stable complex of renin and its inhibitor with a molecular weight of 110,000 was found in cultured neuroblastoma cells indicating the presence of a second type of inactive renin.
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Inagami et al. (1982) studied this question.
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