An Inactive, Prorenin-like Substance in Human Kidney and Plasma
| Autor: | Steven A. Atlas, T. E. Hesson, Jean E. Sealey, John H. Laragh |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Enzyme Precursors
medicine.medical_specialty Kidney Cortex Plasma renin activity Chromatography Affinity Enzyme activator Affinity chromatography Internal medicine Renin Renin–angiotensin system medicine Humans Trypsin biology Chemistry Binding protein fungi General Medicine Enzyme Activation Endocrinology Concanavalin A biology.protein Angiotensin I medicine.drug |
| Zdroj: | Clinical Science. 59:29s-33s |
| ISSN: | 0144-9664 |
| DOI: | 10.1042/cs059029s |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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