Purification of a retinol binding protein from the hen-oviduct cytosol and its immunological cross-reactivity with those from the nucleus

V. R. Prasad, M. R.S. Rao, J. Ganguly

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2 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)271-277
Number of pages7
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number2
Publication statusPublished - Oct 28 1983
Externally publishedYes



  • (Hen oviduct)
  • Antibody
  • Retinol-binding protein, Immunological cross-reactivity

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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