JBC INTERFERin siRNA transfection reagent

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Biochemistry of Visual Pigments

I. PURIFICATION AND PROPERTIES OF BOVINE RHODOPSIN

Hitoshi Shichi 1, Marc S. Lewis 1, Filadelfo Irreverre 2, and Audrey L. Stone 3

From the 1 From the Ophthalmology Branch, National Institute of Neurological Diseases and Blindness, National Institutes of Health, Bethesda, Maryland 20014
2 From the Laboratory of Biophysical Chemistry, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland 20014
3 From the Laboratory of Neurochemistry, National Institute of Mental Health, United States Department of Health, Education, and Welfare, Bethesda, Maryland 20014

Bovine rhodopsin prepared by extraction from retinal outer segments with a nonionic detergent and chromatographic purification on calcium phosphate and ECTEOLA-cellulose migrated electrophoretically as a single band on polyacrylamide gel. The preparation showed spectral ratios of A400:A498 = 0.168 and A280:A498 = 1.75. By amino acid analysis the pigment gave a molecular weight of 28,000 per mole. The 190 and 276 mµ absorption of rhodopsin increased slightly on bleaching. Optical rotatory dispersion and circular dichroism measurements on the highly purified rhodopsin preparation indicate that native rhodopsin possesses approximately 60% helical structure and one-fifth of the helical content is lost on irreversible bleaching. The light-induced conformational change, however, is not observed with outer segments.

Submitted on August 29, 1968


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