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Renin cleavage of a human kidney renin substrate analogous to human angiotensinogen, H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Ser-OH, that is human renin specific and is resistant to cathepsin D
Authors:Martin Poe   Joseph K. Wu   Tsau-Yen Lin   Karst Hoogsteen   Herbert G. Bull  Eve E. Slater
Affiliation:1. Department of Biophysics, Merck, Sharp & Dohme Research Laboratories, Rahway, New Jersey 07065 USA;2. Department of Biochemistry, Merck, Sharp & Dohme Research Laboratories, Rahway, New Jersey 07065 USA;3. Department of Biochemical Endocrinology, Merck, Sharp & Dohme Research Laboratories, Rahway, New Jersey 07065 USA
Abstract:A synthetic tetradecapeptide, H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Ser-OH, which corresponds to the 13 amino terminal residues of human angiotensinogen plus a carboxy terminal serine to replace a suggested site of carbohydrate attachment, has been shown to be a good substrate for human kidney renin. At pH 7.2 and 37 degrees C the KM or Michaelis constant was 8.4 +/- 2.9 microM, and the VM or velocity at infinite tetradecapeptide concentration was 11.3 +/- 2.4 mumol angiotensin I made per hour per milligram renin. The tetradecapeptide was highly resistant to cleavage by mouse submaxillary renin. The tetradecapeptide was also slowly cleaved by human liver cathepsin D, by rabbit lung angiotensin-converting enzyme, and by reconstituted human serum, but did not yield angiotensin I. Thus, this synthetic renin substrate should permit more specific measurement of human kidney renin activity.
Keywords:renin   renin assay   angiotensinoge   angiotensin I   tetradecapeptide renin substrate   cathepsin D-resistant
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