The Tohoku Journal of Experimental Medicine
Online ISSN : 1349-3329
Print ISSN : 0040-8727
ISSN-L : 0040-8727
Purification of Rat Retinol-Binding Protein Using Blue Sepharose CL-6B
KYOSUKE MASAKIYUTAKA WAKOTAKASHI URANOSHUICHI KIMURA
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1986 年 150 巻 3 号 p. 249-257

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MASAKI, K., WAKO, Y., URANO, T. and KIMURA, S. Purification of Rat Retinol-Binding Protein Using Blue Sepharose CL-6B. Tohoku J. exp. Med., 1986, 150 (3), 249-257-Studies were conducted to isolate rat plasma retinol-binding protein, the specific transport protein for vitamin A in the rat. Retinol-binding protein was isolated from rat plasma by a new simple procedure using Blue Sepharose CL-6B, and highly purified retinol-binding protein was obtained. This procedure included DEAE-cellulose chromatography at pH 6.0, Sephadex G-75 gel filtration in the presence of 3.0M urea, Blue Sepharose CL-6B affinity chromatography at pH 7.0 and finally Sephadex G-100 gel filtration at pH 7.4. The third step completely accomplished the dissociation and separation of retinon-binding protein from its complex with prealbumin and plasma albumin. This procedure is a significant improvement over previously published procedures, in which sample recycling and preparative polyacrylamide gel electrophoresis are necessary. The molecular weight, electrophoresic behaviour, ultraviolet and fluorescence spectra of the retinol-binding protein were similar to those appearing in other reports.
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