Premium
Chemisch‐spezifische Kopplung von Adrenocorticotropin‐ und Angiotensin‐II‐Derivaten an Polymerträger für die Affinitätschromatographie
Author(s) -
Fauchère JeanLuc,
Pelican GiatgenMario
Publication year - 1975
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.19750580713
Subject(s) - chemistry , angiotensin ii , covalent bond , asparagine , affinity chromatography , cysteine , peptide , peptide hormone , stereochemistry , chromatography , hormone , amino acid , biochemistry , receptor , organic chemistry , enzyme
Specific covalent attachment of adrenocorticotropin and angiotensin II derivatives to polymeric matrices for use in affinity chromatography The purpose of this investigation was to prepare polymer‐supported forms of adrenocorticotropin and angiotensin II with unique points of covalent attachment and presumably low rates of hormone detachment, making them potentially useful for affinity chromatography. Conventional chemical synthesis provided the peptides cysteinyl‐ACTH (5–24) ([4‐cysteine]‐adrenocorticotropin‐(4‐24)‐heneikosipeptide) and cysteinyl‐angiotensin II amide ([I‐N α ‐cysteinyl‐asparagine,5‐valine]‐angiotensin II). Strategies were devised to bind these hormone derivatives either in the protected form to polyacrylamide or in the deprotected form to sepharose beads. The obtained high degree of matrix substitution suggests a general applicability of these methods.