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Tritiated peptides. Part 10 1 . Catalytic exchange labelling of β‐corticotrophin‐ (1‐24) ‐tetracosapeptide
Author(s) -
Brundish Derek E.,
Wade Roy
Publication year - 1981
Publication title -
journal of labelled compounds and radiopharmaceuticals
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0362-4803
DOI - 10.1002/jlcr.2580180807
Subject(s) - chemistry , tritium , methionine , tyrosine , phenylalanine , residue (chemistry) , labelling , tryptophan , histidine , amino acid , catalysis , stereochemistry , biochemistry , physics , nuclear physics
β‐Corticotrophin‐ (1‐24) ‐tetracosapeptide β‐Corticotrophin‐(1‐24)‐tetracosapeptide: tetracosactrin, Synacthen® (trade name of CIBA‐GEIGY Basle) Ser‐Tyr‐Ser‐Met‐Glu‐His‐Phe‐Arg‐Trp‐Gly‐Lys‐Pro‐Val‐Gly‐Lys‐Lys‐Arg‐Arg‐Pro‐Val‐Lys‐Val‐Tyr‐Pro. was labelled to a level of 0.48 Ci mmol −1 by catalytic exchange of a protected synthetic precursor with tritium gas. Over 80% of the isotope was incorporated into acid‐stable sites in the histidine residue. Smaller amounts were incorporated into methionine (5%), tyrosine (3%), phenylalanine (5%) and tryptophan (2%). Aminobutyric acid was formed (1%) by degradation of methionine and had incorporated tritium (5%). The labelled amino acid residues were stereochemically pure within the limits of experimental error.