Prasad, VR and Rao, MRS and Ganguly, J (1983) Purification of a Retinol Binding Protein From the Hen Oviduct Cytosol and its Immunological Cross-Reactivity with those from the Nucleus. In: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 778 (2). pp. 271-277.
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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 retinoi-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.
|Item Type:||Journal Article|
|Additional Information:||Copyright belongs to Elsevier.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||19 Jun 2008|
|Last Modified:||19 Sep 2010 04:46|
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