[Visual rhodopsin. III. Complete amino acid sequence and topography in a membrane].
Tryptic hydrolysis of apomembranes, BNPS-skatole cleavage of carboxymethylated rhodopsin and thermolytic digestion of native membranes were carried out to obtain the peptides necessary for the polypeptide chain reconstruction. Gel-filtration on Bio-Gel P-30 in 80% formic acid, ion-exchange and reversed-phase high performance liquid chromatography were used for the peptide isolation. A comparison of rhodopsin hydrophobicity profile with the accessibility of the polypeptide chain in native photoreceptor membranes for proteases allowed to distinguish seven alpha-helical segments and propose a model for arrangement of the protein molecule in the membrane.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002462:Cell Membrane / Q000032:analysis; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D010455:Peptides / Q000032:analysis*; D010786:Photoreceptor Cells / Q000032:analysis*; D011487:Protein Conformation; D012168:Retinal Pigments / Q000032:analysis*; D012243:Rhodopsin / Q000032:analysis*; D013820:Thermolysin; D014357:Trypsin
D010455:Peptides; D012168:Retinal Pigments; D012243:Rhodopsin; D014357:Trypsin; D013820:Thermolysin
Zritel'nyĭ rodopsin. III. Polnaia aminokislotnaia posledovatel'nost' i topografiia v membrane.