Isolation and characterization of a biotin-binding protein from the pregnant-rat serum and comparison with that from the chicken egg-yolk.

Seshagiri, Polani B and Adiga, Radhakantha P (1987) Isolation and characterization of a biotin-binding protein from the pregnant-rat serum and comparison with that from the chicken egg-yolk. In: Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology, 916 (3). pp. 474-481.

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Abstract

A biotin-binding protein exhibiting partial immunol. cross-reactivity with the purified chicken egg yolk biotin-binding protein was detected, for the 1st time, in the serum of pregnant/estrogenized female rats but not of normal males. This protein, purified by affinity chromatog. on biotin-AH-Sepharose, was homogeneous by electrophoretic and immunol. criteria. It was a glycoprotein of mol. wt. 66,000 without any detectable subunits, had a pI of 4.1, and specifically bound [14C]biotin. Several structural and functional features of the biotin-binding protein of rat and chicken were similar. These included immunol. cross-reactivity, acidic and glycoprotein nature, the ability to bind tightly [14C]biotin, estrogen stimulation for their appearance in the circulation, and the pattern of distribution of radioiodinated peptides upon proteolysis with trypsin.

Item Type:	Journal Article
Publication:	Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Keywords:	previous termBiotin binding proteinnext term;Immunological crossreactivity;Ligand previous termbinding;Proteinnext term purification;(previous termPregnant rat);(Chicken egg yolk)
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	06 Mar 2008
Last Modified:	01 Mar 2012 07:38
URI:	http://eprints.iisc.ac.in/id/eprint/13154

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