Abstract
Hog kidneyswere minced, lyophilized, extracted with acetone/water, and the extract was gel-filtrated. The partly purified renin was used for analytical ultracentrifugation and for electrofocusing. By these methods the molecular weight of renin was determined to be 4 × 104g/M. Four distinct fractions of enzymatically and immunologically identical renin with pI's between pH 4.75–5.10 were shown. Activation of renin by treatment with acid at pH 3.7 was investigated by means of inhibitors and activators of proteolytic enzymes.

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