Simultaneous purification of biotin-binding proteins-I and -II from chicken egg yolk and their characterization

Subramanian, N and Adiga, PR (1995) Simultaneous purification of biotin-binding proteins-I and -II from chicken egg yolk and their characterization. In: Biochemical Journal, 308 (part 2). pp. 573-577.

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Abstract

Chicken egg yolk biotin-binding protein-I (BBP-I) has been purified to homogeneity along with the tetrameric BBP-II by a common protocol. The purification includes delipidation of egg yolk by butanol extraction, DEAE-Sephacel chromatography, treatment with guanidinium chloride and biotin-aminohexyl-Sepharose affinity chromatography. The identity of purified BBP-I was ascertained by its physicochemical properties as well as by its immunological cross-reactivity and precursor-product relationship with BBP-II.

Item Type:	Journal Article
Additional Information:	Copyright of this article belongs to Portland Press.
Department/Centre:	Division of Biological Sciences > Biochemistry Division of Biological Sciences > Molecular Reproduction, Development & Genetics (formed by the merger of DBGL and CRBME)
Date Deposited:	26 May 2011 07:29
Last Modified:	02 Nov 2011 07:48
URI:	http://eprints.iisc.ernet.in/id/eprint/37898

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