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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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|
|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|
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