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Synthèse de la Val 5 ‐ D ‐Phe 8 ‐angiotensine‐I et nouvelle synthèse de la Val 5 ‐angiotensine‐I
Author(s) -
Guttmann St.
Publication year - 1961
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19610440317
Subject(s) - chemistry , renin–angiotensin system , angiotensin ii , enzyme , angiotensin converting enzyme , stereochemistry , biochemistry , receptor , medicine , blood pressure
Val 5 ‐angiotensin‐I and one of its optical isomers, Val 5 ‐ D ‐Phe 8 ‐angiotensin‐I, were synthesized by a new way excluding any possibility of racemisation. The optical purity of the intermediary and final peptides was furthermore ascertained by enzymatic degradation. Val 5 ‐angiotensin‐I exhibited the full biological activity expected. Val 5 ‐ D ‐Phe 8 ‐angiotensin‐I was found to be practically inactive. It failed also to antagonize Val 5 ‐ or Ileu 5 ‐angiotensin‐I or to inhibit «converting enzyme».