Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated.
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.
Ovchinnikov YuA
Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, Moscow.
Abdulaev
N G
NG
Bogachuk
A S
AS
D000215:Acylation; D000818:Animals; D002417:Cattle; D002462:Cell Membrane / Q000032:analysis; D002849:Chromatography, Gas; D002851:Chromatography, High Pressure Liquid; D003545:Cysteine / Q000378:metabolism*; D003593:Cytoplasm / Q000032:analysis; D013058:Mass Spectrometry; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism*; D011487:Protein Conformation; D012168:Retinal Pigments / Q000378:metabolism*; D012243:Rhodopsin / Q000378:metabolism*; D012374:Rod Cell Outer Segment / Q000032:analysis
D010169:Palmitic Acids; D010446:Peptide Fragments; D012168:Retinal Pigments; D019308:Palmitic Acid; D012243:Rhodopsin; D003545:Cysteine