Abstract
The pentapeptide pepstatin was found to inhibit the ability of rat spleen pseudorenin to form angiotensin I from tetradecapeptide renin substrate. Dixon and Webb plots showed that this inhibition was noncompetitive in nature. Lineweaver-Burk analysis also showed noncompetitive inhibition. Ki values determined by the three graphical methods ranged from 1.8 to 3.8 × 10-10M. The Km for pseudorenin was determined to be between 0.82 and 1.23 μM. The concentration of enzyme used was estimated to be 3.1 × 10-10M. Pepstatin should prove useful in the future for the analysis and purification of pseudorenin.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 639-641 |
| Number of pages | 3 |
| Journal | Biochemical Pharmacology |
| Volume | 26 |
| Issue number | 7 |
| DOIs | |
| State | Published - Apr 1 1977 |
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