concanavalin-a and sucrose-monolaurate

Guanosine 3',5'-cyclic monophosphate phosphodiesterase (EC 3.1.4.1) in frog rod outer segment prepared by a sucrose stepwise density gradient method was activated by light in the presence of GTP. Rhodopsin in rod outer segment was solubilized with sucrose laurylmonoester and then purified by concanavalin A-Sepharose column. Addition of photo-bleached preparation of the purified rhodopsin to the crude rod outer segment, which had been prepared by 43% (w/w) sucrose floatation, caused the activation of phosphodiesterase in the dark, while each component of the photo-product eluted from the column (all-trans retinal and opsin) did not. Regenerated rhodopsin prepared from 11-cis retinal and purified opsin activated phosphodiesterase when it was bleached. From these facts it is suggested that an intermediate or a process of photolysis of rhodopsin causes activation of phosphodiesterase.

Topics: 3',5'-Cyclic-GMP Phosphodiesterases; Animals; Centrifugation, Density Gradient; Chromatography, Affinity; Concanavalin A; Enzyme Activation; Octoxynol; Photic Stimulation; Photolysis; Photoreceptor Cells; Polyethylene Glycols; Rana catesbeiana; Retinal Pigments; Rhodopsin; Rod Cell Outer Segment; Sucrose