[Primary structure of rhodopsin. II. Chymotrypsin hydrolysis peptides].
Apomembranes prepared from the photoreceptor disks were subjected to chymotryptic hydrolysis. The insoluble material, containing the membrane-bound peptides was removed by centrifugation, and the water-soluble peptides of the supernatant were separated by ion-exchange chromatography on AG 50W X 4 followed by high performance liquid chromatography. The insoluble peptides were separated by gel-filtration on Bio-Gel P-30 in 80% formic acid. Amino acid sequence of peptides containing in total 296 amino acid residues and comprising 85% of the rhodopsin polypeptide chain was determined.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin; D006868:Hydrolysis; D010455:Peptides / Q000032:analysis*; D010786:Photoreceptor Cells / Q000032:analysis; D012168:Retinal Pigments / Q000032:analysis*; D012243:Rhodopsin / Q000032:analysis*
D010455:Peptides; D012168:Retinal Pigments; D012243:Rhodopsin; D002918:Chymotrypsin
Pervichnaia struktura rodopsina. II. Peptidy khimotripticheskogo gidroliza.