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1. A simple, efficient three-step method for purification of serum retinol-binding-protein is described with homogeneity obtained after chromatography on DEAE-Sephadex, CM-Sephadex and Sephadex G-100. 2. Evidence is presented indicating that retinol receptors present in the cytosol fraction of chick retina and pigment epithelium are separate and distinct from purified retinol-binding protein. Fluorescence characteristics are different in tissue cytosol and serum as assessed by sucrose density gradient analysis. Tissue retinol receptors do not interact with human serum prealbumin although the prealbumin readily complexes with purified chicken retinol-binding protein. Likewise, no binding to serum retinol-binding protein antibody could be detected by sucrose density gradient analysis, in immunoprecipitation experiments or by double immunodiffusion. It thus appears that specific retinol receptors are present in neural retina and pigment epithelium that are different from serum retinol-binding protein.
T Abe, and
B Wiggert, and
D R Bergsma, and
G J Chader
December 1977,
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T Abe, and
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G J Chader
January 1982,
Vision research,
T Abe, and
B Wiggert, and
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G J Chader
January 1979,
Current topics in eye research,
T Abe, and
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G J Chader
July 1986,
Investigative ophthalmology & visual science,
T Abe, and
B Wiggert, and
D R Bergsma, and
G J Chader
December 1980,
Investigative ophthalmology & visual science,
T Abe, and
B Wiggert, and
D R Bergsma, and
G J Chader
October 1975,
Investigative ophthalmology,
T Abe, and
B Wiggert, and
D R Bergsma, and
G J Chader
May 1976,
Experimental eye research,
T Abe, and
B Wiggert, and
D R Bergsma, and
G J Chader
July 1991,
Experimental eye research,
T Abe, and
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D R Bergsma, and
G J Chader
September 2002,
The Journal of nutrition,
T Abe, and
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D R Bergsma, and
G J Chader
January 1977,
Nature,
