Seshagiri, Polani B. ; Adiga, P. Radhakantha (1987) Isolation and characterisation of a biotin-binding protein from the pregnant-rat serum and comparison with that from the chicken egg-yolk Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, 916 (3). pp. 474-481. ISSN 0167-4838
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Official URL: http://linkinghub.elsevier.com/retrieve/pii/016748...
Related URL: http://dx.doi.org/10.1016/0167-4838(87)90194-4
Abstract
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.
Item Type: | Article |
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Source: | Copyright of this article belongs to Elsevier Science. |
Keywords: | Biotin Binding Protein; Immunological Crossreactivity; Ligand Binding; Protein Purification; (Pregnant Rat); (Chicken Egg Yolk) |
ID Code: | 26811 |
Deposited On: | 08 Dec 2010 13:08 |
Last Modified: | 13 May 2011 04:31 |
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