Purification of a retinol binding protein from the hen-oviduct cytosol and its immunological cross-reactivity with those from the nucleus.
Cellular retinol-binding protein was purified from the cytosol of the oviducts of laying hens by ammonium sulphate fractionation and chromatography on Sephadex G-75 and DEAE-Sephadex A-50 columns. Analysis of the purified retinol-binding protein on 10% SDS-polyacrylamide gel revealed the presence of a doublet representing very similar molecular sizes. Antiserum was prepared against the purified cellular retinol-binding protein, and on the basis of (a) immunodiffusion test and (b) immunoneutralization of 3H-labelled retinol-cellular retinol-binding protein complex on a column of Sephadex G-75, the antiserum appeared to be specific. The antiserum showed cross-reactivity with the nucleosol and a 0.4 M NaCl extract of the chromatin of the oviduct nuclei, while it did not react with the major egg-white proteins such as ovalbumin, conalbumin and ovomucoid.
D000818:Animals; D000936:Antigen-Antibody Complex; D002467:Cell Nucleus / Q000378:metabolism; D002645:Chickens; D003429:Cross Reactions; D003600:Cytosol / Q000378:metabolism; D005260:Female; D007106:Immune Sera; D005779:Immunodiffusion; D010057:Oviducts / Q000378:metabolism*; D012177:Retinol-Binding Proteins / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D054840:Retinol-Binding Proteins, Cellular; D014801:Vitamin A / Q000378:metabolism
D000936:Antigen-Antibody Complex; D007106:Immune Sera; D012177:Retinol-Binding Proteins; D054840:Retinol-Binding Proteins, Cellular; D014801:Vitamin A