[Purification and partial sequence of a hydrophobic polypeptide from BNPS-skatole cleaved bovine rhodopsin].
Rhodopsin isolated from outer segments of cattle retinas was cleaved at tryptophan residues by the BNPS-skatole. One of the polypeptides obtained S 5 (molecular weight about 12,000) of hydrophobic nature was isolated and the sequence of its 50 first residues revealed 60% of hydrophobic AA.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D012168:Retinal Pigments / Q000302:isolation & purification*; D012243:Rhodopsin / Q000302:isolation & purification*; D012862:Skatole / Q000031:analogs & derivatives; D013434:Sulfenic Acids
D010446:Peptide Fragments; D012168:Retinal Pigments; D013434:Sulfenic Acids; C005904:BNPS-skatole; D012243:Rhodopsin; D012862:Skatole
Purification et séquence partielle d'un polypeptide hydrophobe de la rhodopsine bovine fragmentée par le BNPS-scatole.