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pubmed:abstractText |
In the visual pigment, the chromophore retinal is bound through a Schiff base linkage with the protein moiety, opsin. The secondary interaction of retinal with opsin was studied in cephalopod rhodopsin and its photoproduct, metarhodopsin. The pK of the protonation of the Schiff base in metarhodopsin was affected by the phospholipids and detergents surrounding the protein, and varied between 9.2 and 6.9. Among nonionic detergents, the fatty acid ester of sucrose behaved like phospholipids but other detergents changed the protein conformation so that the pK of the Schiff base in metarhodopsin became nearly equal to the pK of N-retinylidene butylamine. This tendency was manifested in rhodopsin as the formation of a 380 nm pigment.
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