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Is the C‐terminal flanking peptide of rat cholecystokinin double sulphated?
Author(s) -
Adrian T.E.,
Domin J.,
Bacarese-Hamilton A.J.,
Bloom S.R.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80203-4
Subject(s) - cholecystokinin , peptide , serine , chemistry , radioimmunoassay , tyrosine , biochemistry , peptide sequence , amino acid , microbiology and biotechnology , biology , receptor , gene , enzyme
A specific radioimmunoassay was developed to the predicted nine amino acid C‐terminal flanking peptide of cholecystokinin (peptide serine serine, PSS). In aqueous extracts of rat brain, PSS was undetectable unless the extracts were first treated with arylsulphatase, which also resulted in desulphation of cholecystokinin. The reverse‐phase HPLC analysis of partially desulphated extracts showed the presence of two peaks intermediate to the naturally occurring and the completely desulphated forms. It is therefore proposed that the CCK‐flanking peptide PSS has both tyrosine residues sulphated.