The membrane bound retinol dehydrogenase from bovine rod outer segments |
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Authors: | William S Blaner Jorge E Churchich |
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Affiliation: | Department of Biochemistry, University of Tennessee Knoxville, Tennessee 37916 USA |
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Abstract: | Retinol dehydrogenase from bovine rod outer segments was solubilized in detergent and partially purified 25-fold through a combination of hydroxyapatite and retinyl-Sepharose chromatography. Alltrans retinol solubilized in protein solutions of bovine serum albumin or β-lactalbumin was a better substrate for the enzyme than retinol solubilized in detergents or suspended in buffer. Retinol dehydrogenase was sensitive to the carbonyl reagent pyridoxal-5′-phosphate but was not inhibited by retinal followed by reduction with NaBH4. The solubilized enzyme requires phospholipids to maintain enzymatic activity, as was evidenced by the inactivating effect of phospholipase A2 on the partially purified enzyme. |
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