Chemical cleavage of bovine rhodopsin at tryptophanyl bonds; characterization of the polypeptide fragments and the phosphorylated site.
Bovine rhodopsin from retinal rod photoreceptors, a protein of 39,000 molecular weight, was cleaved by BNPS-Skatole at the level of tryptophanyl bonds. This hydrolysis yields five fragments S1, S2, S3, S4 and S5 (molecular weights: 35,000, 28,000, 19,500, and 15,500 and 12,000, respectively) and four peptides. Large fragments were purified by polyacrylamide gel electrophoresis in SDS. S2, S3 and S4 contain the glycanes of native rhodopsin and their N-termini are blocked. S5 has the same C-terminal extremity as rhodopsin and contains the phosphorylated site. Phosphate groups are incorporated in this fragment on serines and threonines.
D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010766:Phosphorylation; D012168:Retinal Pigments; D012243:Rhodopsin; D014364:Tryptophan
D010446:Peptide Fragments; D012168:Retinal Pigments; D014364:Tryptophan; D012243:Rhodopsin