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. 1995 Jun 1;308 ( Pt 2)(Pt 2):573-7.
doi: 10.1042/bj3080573.

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

N Subramanian  1 , P R Adiga
Affiliations

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

N Subramanian et al. Biochem J. .

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.

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