[Visual rhodopsin. III. Complete amino acid sequence and topography in a membrane]

Autor: Iu A, Ovchinnikov, N G, Abdulaev, M Iu, Feĭgina, I D, Artamonov, A S, Bogachuk
Rok vydání: 1983
Předmět:
Zdroj: Bioorganicheskaia khimiia. 9(10)
ISSN: 0132-3423
Popis: 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.
Databáze: OpenAIRE