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Purification of human plasma retinol-binding protein by hydrophobic interaction chromatography

✍ Scribed by Rodolfo Berni; Simone Ottonello; Hugo L. Monaco

Publisher
Elsevier Science
Year
1985
Tongue
English
Weight
332 KB
Volume
150
Category
Article
ISSN
0003-2697

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✦ Synopsis

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. o 198s Aademrc

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