Affinity labeling of bovine opsin by trans-retinoyl chloromethane.
All-trans-retinoyl chloromethane is a potent irreversible inactivator of bovine opsin in retinal rod outer segments. The inactivation appears to be due to specific modification of the apoprotein at the 11-cis-retinaldehyde binding site. The reaction follows pseudo first order kinetics at 37 degrees C. A moderate dissociation constant for the initial reversible complex of 6.1 mM could be derived with a first order rate constant of 1.8x10(-1) min-1 for the conversion to the irreversible inactivated form. Native rhodopsin or rhodopsin regenerated from opsin by addition of 11-cis-retinaldehyde is completely protected against inactivation by trans-retinoyl chloromethane. All-trans-retinaldehyde does not provide this protection for the irreversible inactivation.
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Department of Biochemistry and Ophthalmology, Tulane University Medical Center, New Orleans, LA 70112.
Schoellmann
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D000345:Affinity Labels; D000818:Animals; D002417:Cattle; D005136:Eye Proteins / Q000378:metabolism*; D007700:Kinetics; D012172:Retinaldehyde; D012374:Rod Cell Outer Segment / Q000378:metabolism; D017299:Rod Opsins; D014212:Tretinoin / Q000031:analogs & derivatives / Q000494:pharmacology
D000345:Affinity Labels; D005136:Eye Proteins; D017299:Rod Opsins; D014212:Tretinoin; C059489:trans-retinoyl chloromethane; D012172:Retinaldehyde