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Insight into covalent modifications of rhodopsin shows palmitic acid attachment in bovine rhodopsin.
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.
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Ovchinnikov et al. (1988) studied this question.
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