A Protein-Bound Form of Porcine Renal Renin

¹ Medical Unit, St. Mary's Hospital Medical School, Norfolk Place, London, W.2, Great Britain

Two interconvertible renins were isolated from extracts of the pig renal cortex at neutral pH and shown to be protein-bound (renin B, molecular weight 60,000) and free (renin A, molecular weight 40,000) forms of renin. The protein-bound form (renin B) gave a much more prolonged pressor response than did the free form (renin A) on direct bioassay in the rat; it could be converted to renin A by the action of various salts or by acidification below pH 3. The renin-binding protein associated with renin B was isolated by DEAE-cellulose column chromatography under special conditions of elution and appeared to be specific for renin. When pig kidneys were perfused in situ with Krebs-Ringer's solution, isoproterenol stimulation (1-8 µg/min) resulted in release of renin in the protein-bound form. It is suggested that renin-binding protein may act as a carrier for the transport of renin to local tissue sites of uptake under some circumstances and thus alter the mode of expression of the renin-angiotensin system in vivo to one of local angiotensin generation and effect.

Submitted on July 10, 1973
Accepted on May 31, 1974

This article has been cited by other articles:

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