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.
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Research Article| October 01 1979
The incorporation of tritiated retinyl moiety into the active-site lysine residue of bacteriorhodopsin
Biochem J (1979) 183 (1): 175–178.
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E Mullen, M G Gore, M Akhtar; The incorporation of tritiated retinyl moiety into the active-site lysine residue of bacteriorhodopsin. Biochem J 1 October 1979; 183 (1): 175–178. doi: https://doi.org/10.1042/bj1830175
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