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

FEBS Lett. 1988 Mar 28;230(1-2):1-5. doi: 10.1016/0014-5793(88)80628-8.

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.

MeSH terms

  • Acylation
  • Animals
  • Cattle
  • Cell Membrane / analysis
  • Chromatography, Gas
  • Chromatography, High Pressure Liquid
  • Cysteine / metabolism*
  • Cytoplasm / analysis
  • Mass Spectrometry
  • Palmitic Acid
  • Palmitic Acids / metabolism*
  • Peptide Fragments / isolation & purification
  • Peptide Fragments / metabolism*
  • Protein Conformation
  • Retinal Pigments / metabolism*
  • Rhodopsin / metabolism*
  • Rod Cell Outer Segment / analysis

Substances

  • Palmitic Acids
  • Peptide Fragments
  • Retinal Pigments
  • Palmitic Acid
  • Rhodopsin
  • Cysteine