-transparent.png){kind=logo}
A biotin-binding protein exhibiting partial immunological cross-reactivity with the purified chicken egg-yolk biotin-binding protein has been detected, for the first time, in the sera of pregnant/estrogenised female rats but not of the normal males. This protein, purified by affinity chromatography on a biotin-AH-Sepharose was homogeneous by electrophoretic and immunological criteria. It was a glycoprotein of Mr 66,000 without any detectable subunites, had a pI 4.1, and specifically bound [14C]biotin. Several structural and functional features of the biotin-binding protein of rat and chicken were found to be similar. These included immunological cross-reactivity, acidic and glycoprotein nature, ability to tightly bind [14C]biotin, estrogen stimulation for their appearance in circulation, and the pattern of distribution of radioiodinated peptides upon proteolysis with trypsin.
P B Seshagiri, and
P R Adiga
May 1984,
Biochimica et biophysica acta,
P B Seshagiri, and
P R Adiga
August 1976,
The Biochemical journal,
P B Seshagiri, and
P R Adiga
October 1978,
The Journal of biological chemistry,
P B Seshagiri, and
P R Adiga
November 1978,
The Biochemical journal,
P B Seshagiri, and
P R Adiga
January 1979,
Methods in enzymology,
P B Seshagiri, and
P R Adiga
March 1981,
The Biochemical journal,
P B Seshagiri, and
P R Adiga
June 1995,
The Biochemical journal,
P B Seshagiri, and
P R Adiga
September 1989,
Biochimica et biophysica acta,
P B Seshagiri, and
P R Adiga
December 1986,
Proceedings of the National Academy of Sciences of the United States of America,
P B Seshagiri, and
P R Adiga
May 1980,
The Biochemical journal,
