Purification of cellular retinaldehyde-binding protein from bovine retina and retinal pigment epithelium.
Cellular retinaldehyde-binding protein (CRALP) has been purified from extracts of bovine retina or retinal pigment epithelium by a procedure employing an initial, high-capacity anion exchange chromatographic step and anion exchange HPLC for removal of a persistent contaminant. The procedure also yields fractions containing three other retinoid-binding proteins present in retina (cellular retinol-, cellular retinoic acid- and interphotoreceptor retinol-binding proteins; CRBP, CRABP and IRBP, respectively). Procedures are described for labeling CRALBP with 9-cis-retinaldehyde, 11-cis-retinaldehyde, or 11-cis-retinol. There are approx. 3 nmol of CRALBP per adult bovine eye and the binding protein is ca. 0.5% of the soluble protein of a retinal supernatant.[1]References
- Purification of cellular retinaldehyde-binding protein from bovine retina and retinal pigment epithelium. Saari, J.C., Bredberg, D.L. Exp. Eye Res. (1988) [Pubmed]
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