Purification and partial characterization of a novel cellular retinol-binding protein, type three, from the piscine eyes |
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| Authors: | S Nishiwaki M Kato M Okuno M Kanai Y Muto |
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| Affiliation: | First Department of Internal Medicine, Gifu University School of Medicine, Japan. |
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| Abstract: | A novel cellular retinol-binding protein, termed type three (CRBP III), was isolated from eyes of the bigeye of tuna. CRBP III showed a molecular weight of 15,400, an isoelectric point of 4.80, alpha 1-mobility in electrophoresis, and a lambda max of 350 nm. All-trans-retinol, the endogenous ligand, could be competitively displaced by retinoic acid but not by retinal. CRBP III was differentiated from purified piscine and rat cellular retinol-binding proteins (CRBP) and cellular retinoic acid-binding proteins (CRABP) by its amino-acid composition, electrophoretic mobility, fluorescence spectra and ligand-binding specificity. |
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