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A rapid and large-scale isolation of renin from mouse submaxillary gland by pepstatin-aminohexyl-agarose affinity chromatography


A rapid and large-scale isolation of renin from mouse submaxillary gland by pepstatin-aminohexyl-agarose affinity chromatography



Journal of Biochemistry 89(4): 1107-1112



ISSN/ISBN: 0021-924X

PMID: 7019205

A pressor enzyme, renin, was purified about 60-fold by chromatography on an affinity column including pepstatin-aminohexyl-agarose with a high yield of 83% from the homogenate of adult mouse submaxillary glands. The renin obtained by the one-step purification was electrophoretically homogenous on SDS-polyacrylamide gel and was as active as an absolutely pure renin. The renin purified by the affinity column could be separated into five active components by chromatography on CM-cellulose. Each of these renins gave a symmetrical elution profile on the CM-cellulose column and a discrete protein band on polyacrylamide gel electrophoresis at pH 8.6. Administration of nanogram quantities of each of the two major renin fractions to nephrectomized rats caused a sustained rise of blood pressure and decrease in sensitivity of the animal to angiotensin II. This rapid and large-scale purification method using pepstatin-aminohexyl-agarose eliminates all four fractionation steps reported previously for the isolation of mouse submaxillary gland renin.

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Accession: 014900853

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Related references

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