Partial purification of human renin.

Abstract:

:An affinity gel for the purification of renin was prepared by coupling pepstatin to aminohexylagarose gel. Partially purified human renin (Haas et al., Arch. Biochem. Biophys., 110, 534-543, 1965) was purified further by affinity chromatography on the pepstatin-aminohexyl-agarose gel, gel filtration on a Sephadex G-75 column, and ion exchange chromatography on a DEAE-cellulose column. Separation from a protease permitted further purification without progressive loss of activity. Three peaks of enzymatically active renin were obtained after the DEAE-cellulose chromatography, with specific activities ranging from 206 to 166 and 85 Goldblatt units/mg protein, respectively. The specific activity of 206 GU units/mg represents a 103,000-fold purification compared to the renin present in the first crude extract.

journal_name

Circ Res

journal_title

Circulation research

authors

Murakami K,Inagami T,Haas E

doi

10.1161/01.res.41.4.4

subject

Has Abstract

pub_date

1977-10-01 00:00:00

pages

4-7

issue

4 Suppl 2

eissn

0009-7330

issn

1524-4571

journal_volume

41

pub_type

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