Purification of a Retinol Binding Protein From the Hen Oviduct Cytosol and its Immunological Cross-Reactivity with those from the Nucleus

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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Abstract

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
Publication:	Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Publisher:	Elsevier Science B.V
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
URI:	http://eprints.iisc.ac.in/id/eprint/14532

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