Two adjacent cysteine residues in the C‐terminal cytoplasmic fragment of bovine rhodopsin are palmitylated

Yu.A. Ovchinnikov; N.G. Abdulaev; A.S. Bogachuk

doi:10.1016/0014-5793(88)80628-8

March 28, 1988FEBS LettersOpen Access

Two adjacent cysteine residues in the C‐terminal cytoplasmic fragment of bovine rhodopsin are palmitylated

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Key Points

This research investigates the modification of cysteine residues in the cytoplasmic fragment of rhodopsin.
Used covalent coupling of bovine rhodopsin to CPG-thiol glass for peptide separation.
Identified modifications in the C-terminal cytoplasmic fragment through CNBr peptide analysis.
Cysteine residues 322 and 323 in the cytoplasmic fragment of rhodopsin were modified with palmitic acid.

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Implication

Insight into covalent modifications of rhodopsin shows palmitic acid attachment in bovine rhodopsin.

Abstract

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.

synapsesocial.com/papers/6a20902405ff00c089b41c21 https://doi.org/10.1016/0014-5793(88)80628-8

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Two adjacent cysteine residues in the C‐terminal cytoplasmic fragment of bovine rhodopsin are palmitylated

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

Two adjacent cysteine residues in the C‐terminal cytoplasmic fragment of bovine rhodopsin are palmitylated

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

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