title: An inactive, prorenin-like substance in human kidney and plasma.
abstract: 1. Plasma prorenin (inactive renin), which accounts for about 70% of the total renin in human plasma, was almost completely separated from active renin by affinity chromatography on Cibacron blue F3G-A-agarose. The slight residual renin activity present in the prorenin peak can be removed on concanavalin A-Sepharose, demonstrating that prorenin is completely inactive. 2. The renin activity of both human renal cortical extract and renal perfusate increased after incubation with trypsin. This trypsin-activable renin accounted for 15 and 40% of the total renin in extract and perfusate respectively. 3. Trypsin-activable renin from both renal extract and renal perfusate was, like plasma prorenin, almost completely separated from active renin on Cibacron blue F3G-A-agarose. After additional chromatographic steps, the trypsin-activable renin from renal cortical extract was found to be completely inactive. 4. We conclude that human kidney contains, and is able to release, a trypsin-activable renin that resembles plasma prorenin. It may differ from many of the 60 000 molecular-weight forms of renin previously identified in renal extracts, since these possess considerable intrinsic renin activity and probably represent a complex of renin with a binding protein.
mesh_terms: D000803:Angiotensin I / Q000378:metabolism; D002846:Chromatography, Affinity; D004789:Enzyme Activation / Q000187:drug effects; D004792:Enzyme Precursors / Q000097:blood / Q000378:metabolism*; D006801:Humans; D007672:Kidney Cortex / Q000201:enzymology*; D012083:Renin / Q000097:blood / Q000378:metabolism*; D014357:Trypsin / Q000494:pharmacology
chemical_list: D004792:Enzyme Precursors; D000803:Angiotensin I; D014357:Trypsin; D012083:Renin