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Die Synthese von menschlichem adrenocorticotropem Hormon (α h ‐ACTH) mit revidierter Aminosäuresequenz
Author(s) -
Sieber P.,
Rittel W.,
Riniker B.
Publication year - 1972
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.19720550420
Subject(s) - chemistry , deamidation , peptide , stereochemistry , sequence (biology) , peptide sequence , trypsin , biochemistry , enzyme , gene
We demonstrated recently that the amino acid sequence of human ACTH (α h ‐ACTH 1 ) differs in four positions from the structure reported in 1961 by Lee and coworkers. The synthesis of the revised sequence and a method of verifying the identity of the synthetic peptide with the naturally occurring hormone are described. The two preparations can most readily be compared by examining the mixture of fragments obtained upon degradation with trypsin. In this mixture, fragments 22–39 of natural α h ‐ACTH and of the synthetic peptide are identical and easily distinguishable from the corresponding synthetic fragment of the previously postulated sequence. This is demonstrated by thin layer‐chromatography and ‐electrophoresis as well as by reference to the rate of deamidation under alkaline conditions.