Identification and molecular characterisation of a biotin-binding protein distinct from avidin of chicken egg white and comparison with yolk biotin-binding protein

Seshagiri, Polani B. ; Adiga, P. Radhakantha (1987) Identification and molecular characterisation of a biotin-binding protein distinct from avidin of chicken egg white and comparison with yolk biotin-binding protein Biochimica et Biophysica Acta: General Subjects, 926 (3). pp. 321-330. ISSN 0304-4165

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/030441...

Related URL: http://dx.doi.org/10.1016/0304-4165(87)90218-2

Abstract

By immunological and biochemical methods a biotin-binding protein, distinct from avidin, has been shown to be present in chicken egg white. This vitamin-binding protein (Mr 67 000) bound [14C]biotin, displayed thermally induced biotin exchange reaction and exhibited gross immunological cross-reactivity with the purified yolk biotin-binding protein. In vitro labelling of soluble proteins with radioactive amino acids in the oviduct tissue explants from estrogenised chicks revealed that approx. 2% of the total radioactive proteins was immunoprecipitated with anti-yolk biotin-binding protein antibodies. The protein could be purified to homogeneity by employing ion-exchange chromatography on DEAE-cellulose and biotin-AH Sepharose affinity chromatography. The purified protein specifically bound [14C]biotin, and exhibited complete immunological homology with the yolk biotin-binding protein but not with avidin. Its electrophoretic mobility (at pH 8.3), acidic nature, biotin-binding characteristics, immunological cross-reactivity and tryptic peptide maps were very similar to that of yolk biotin-binding protein, and not avidin.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Biotin Binding Protein; Avidin; (Chicken Egg)
ID Code:26792
Deposited On:08 Dec 2010 13:11
Last Modified:13 May 2011 04:32

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