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Two adjacent cysteine residues in the C‐terminal cytoplasmic fragment of bovine rhodopsin are palmitylated
Author(s) -
Ovchinnikov Yu.A.,
Abdulaev N.G.,
Bogachuk A.S.
Publication year - 1988
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(88)80628-8
Subject(s) - rhodopsin , cysteine , chemistry , cytoplasm , covalent bond , biochemistry , retinal , organic chemistry , enzyme
Covalent coupling of bovine rhodopsin to CPG‐thiol glass was used for separation of CNBr peptides. It is shown that cysteine residues 322 and 323 in the C‐terminal cytoplasmic fragment of rhodopsin are modified with palmitic acid.