Rhodopsin reconstitution in bleached rod outer segment membranes in the presence of a retinal-binding protein from the honeybee.
The physiological role of a retinal-binding protein from honeybee is investigated. This protein, upon previous loading with all-trans retinal and subsequent irradiation with monochromatic light of wavelength 490 nm, is able to promote the reconstitution of rhodopsin when added to a suspension of opsin membranes from bleached bovine rod outer segments. In this respect this retinal-binding protein could have a role very similar to that postulated for the well-known cephalopod retinochrome, that serves to catalyze the formation in the presence of light of 11-cis retinal in photo-receptor cells and to provide it for the reconstitution of rhodopsin during the visual cycle.
Pepe
I M
IM
Istituto di Cibernetica e Biofisica del CNR, Genova, Italy.
Cugnoli
C
C
Schwemer
J
J
D000818:Animals; D001516:Bees; D002352:Carrier Proteins / Q000502:physiology*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D005136:Eye Proteins / Q000378:metabolism; D066298:In Vitro Techniques; D012168:Retinal Pigments; D012172:Retinaldehyde / Q000378:metabolism; D012243:Rhodopsin; D012374:Rod Cell Outer Segment; D017299:Rod Opsins; D013057:Spectrum Analysis
C020932:11-cis-retinal-binding protein; D002352:Carrier Proteins; D005136:Eye Proteins; D012168:Retinal Pigments; D017299:Rod Opsins; D012243:Rhodopsin; D012172:Retinaldehyde