Purification and Properties of Bovine Pituitary Renin
Keyword(s):
1. Renin was purified to homogeneity from bovine anterior pituitary by using batchwise DEAE-cellulose chromatography, pepstatin-aminohexyl-agarose affinity chromatography, Ultrogel AcA 44 gel filtration and DEAE-Sephacel and CM-cellulose ion exchange chromatography. 2. The enzyme has a molecular weight of 36 000 and an isoelectric point of 5.25, and exhibits optimum activity at a pH between 6.5 and 7.5. 3. The amino acid composition and antigenic properties of this purified renin are very similar to those of rat, dog and hog kidney renins.
1976 ◽
Vol 35
(03)
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pp. 576-585
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1984 ◽
Vol 62
(6)
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pp. 449-455
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1985 ◽
Vol 63
(11)
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pp. 1160-1166
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1984 ◽
Vol 62
(5)
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pp. 276-279
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