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Biochemical Journal logoLink to Biochemical Journal
. 1990 Jan 1;265(1):301–304. doi: 10.1042/bj2650301

A novel preparative method for the isolation of avidin and riboflavin-binding glycoprotein from chicken egg-white by the use of high-performance liquid chromatography.

V E Piskarev 1, A M Shuster 1, A G Gabibov 1, A G Rabinkov 1
PMCID: PMC1136643  PMID: 2302170

Abstract

A method for the rapid preparative isolation of highly purified avidin using h.p.l.c. on a powerful cation-exchanger TSK SP-5PW column has been developed. The method is based on the following properties of avidin: solubility at a high (NH4)2SO4 concentration, stability and relatively low solubility in organic solvents, as well as the strongly cationic nature of the molecule. Riboflavin-binding glycoprotein may be isolated as by-product.

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Selected References

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