title: The incorporation of tritiated retinyl moiety into the active-site lysine residue of bacteriorhodopsin.
abstract: Purple membranes were isolated from Halobacterium halobium bleached and regenerated with all-trans-[15-3H]retinal. The incorporation of label was 1.2 mol of retinal/mol of bacterio-opsin. The [3H]retinyl-bacterio-opsin obtained from regeneration was hydrolysed to give tritiated retinyl-lysine, which, on hydrogenation to N-epsilon-perhydro[3H]retinyl-lysine and reaction with 1-fluoro-2,4-dinitrobenzene, gave bis-(2,4-dinitrophenyl)-N-epsilon-perhydro[3H]retinyl-lysine. This result confirmed that the retinyl moiety of the chromophore is attached to an epsilon-amino group of lysine.
mesh_terms: D001436:Bacteriorhodopsins / Q000378:metabolism*; D001665:Binding Sites; D002338:Carotenoids / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D006217:Halobacterium / Q000032:analysis; D006868:Hydrolysis; D008239:Lysine / Q000378:metabolism*; D012172:Retinaldehyde / Q000378:metabolism*; D014316:Tritium; D014801:Vitamin A / Q000031:analogs & derivatives*
chemical_list: D014316:Tritium; D014801:Vitamin A; D002338:Carotenoids; D001436:Bacteriorhodopsins; D008239:Lysine; D012172:Retinaldehyde