[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.