Peptide inhibitors of renin angiotensinogen reaction system
| Autor: | Yamamura Yuichi, Hiwada Kunio, Mizoguchi Tomishige, Kokubu Tatsuo, Ito Taketoshi, Ueda Einosuke, Shigezane Keisuke |
|---|---|
| Rok vydání: | 1973 |
| Předmět: |
Kidney Cortex
Stereochemistry Carboxylic acid Sodium chemistry.chemical_element Peptide Blood Pressure Vagotomy Kidney Biochemistry Nephrectomy chemistry.chemical_compound Leucine Amide Renin–angiotensin system Alpha-Globulins Renin Animals Histidine Protein Precursors Pharmacology chemistry.chemical_classification Tetrapeptide Chemistry Angiotensin II Vagus Nerve Valine Peptide Chain Termination Translational Amino acid Kinetics Reaction system Rabbits Sulfonic Acids Peptides Oxidation-Reduction |
| Zdroj: | Biochemical pharmacology. 22(24) |
| ISSN: | 0006-2952 |
| Popis: | Methyl or ethyl esters of synthetic tetrapeptides, Leu-Leu-Val-Tyr and Leu-Leu-Val-Phe, acted as competitive inhibitors in the renin renin-substrate reaction system. The chemical structures needed for the anti-renin activity were presumed to be as follows: (1) a Leu-Leu bond at the N -terminal end of the tetrapeptide; (2) a Leu-Leu bond with L -Leu at the N -terminal end; (3) the presence of Tyr or Phe at the C -terminal end; (4) the replacement of Val in position 3 by Leu did not reduce the activity; (5) the amide formation of the carboxylic acid of the C -terminal amino acid reduced the activity, but deoxidation produced little change in the activity; (6) the coupling of benzyloxycarbonyl or sodium metasulfonic acid group to the N -terminal end markedly reduced the activity; and (7) the addition of His to the N -terminal end caused almost no change in activity. The pressor response produced by renin injected intravenously into a rabbit being treated with an infusion of the tetrapeptide solution was inhibited compared with that in the control animals. |
| Databáze: | OpenAIRE |
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