Extraction,regeneration after bleaching,and ion-exchange chromatography of rhodopsin in Tween 80

Rhodopsin can be readily and somewhat, selectively extracted into Tween 80 solutions from the isolated photoreceptor particulate fraction of bovine retinal tissue. Approximately 80% of the rhodopsin is recovered from the particulate fraction with A₄₉₈ values of approximately 6 and spectral ratios (A₂₇₈:A₄₉₈) of 1.8-1.9. The solutions are estimated to be approximately 97% pure based upon assay of protein and rhodopsin content and 98% pure based upon chromatography on DEAE-cellulose. The bulk of the rhodopsin can be regenerated after bleaching in Tween 80. Partial regenerability is retained when solutions of unbleached or bleached rhodopsin in Tween 80 are further purified by DEAE-cellulose chromatography.