Bovine pituitary renin was successfully purified to homogeneity and demonstrated to have biochemical and antigenic properties similar to kidney renins from other species.
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Supports extrarenal renin in bovine pituitary; extends cross-species data but leaves open human relevance.
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.
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OHSAWA et al. (1982) studied this question.
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