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. 1995 Jun 1;308(Pt 2):573–577. 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 1
PMCID: PMC1136964  PMID: 7772044

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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