Author(s): Berni R, Ottonello S, Monaco HL
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Abstract Human plasma retinol-binding protein has been purified to homogeneity by a simple method that requires an ammonium sulfate fractionation, a hydrophobic interaction chromatography on phenyl-Sepharose, which dissociates the complex between retinol-binding protein and its carrier, transthyretin, and a gel filtration on Sephadex G-50. The yield of pure protein is comparable or higher than that obtained with the more complex procedures previously reported.
This article was published in Anal Biochem
and referenced in Biochemistry & Pharmacology: Open Access