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Purification and Characterization of beta-Lactoglobulin Genetic Variants A and B Using Preparative Electrophoresis and Isoelectric Focusing

is considered as one of the main allergenic components in bovine milk,16, 17, 18 and therefore the modification of βLG is considered as a promising treatment for milk allergy.19 βLG also has good emulsifying and foaming properties, and therefore offers a good model for elucidation of the adsorption characteristics of proteins at a surface. βLG is also a model protein for studying the denaturation mechanism.20, 21 These properties are important in the milk industry and bovine milk allergy.

Purification and analytical separation of the genetic variants of bovine βLG have been carried out by using different chromatographic methods, e.g. ion exchange chromatography with DEAE cellulose and recently HPLC, 22, 23, 24, 25, 26 and also by different electrophoretic methods.27 Many of the above separation methods are either uneconomical or too timeconsuming to be used routinely for large scale purification and phenotyping of dairy cow populations.

We report here a novel method which can be used for both preparative and analytical scale purification of βLG A and βLG B variants with native PAGE by using continuous elution electrophoresis.


Methods
SAMPLE PREPARATION; NATIVE BLG
A mixture of the phenotypes A and B from bovine milk (approximately 80%, lyophilized powder, Sigma Chemical Co., St. Louis, MO, USA) was dissolved in deionized water, pH 7.0 (20 mg/300 l), and the protein concentration of the solution was measured both at 280 nm (Shimadzu UV-1201 spectrophotometer) Ε1%1 cm=9.528 and by using Bio-Rads Protein Assay (Bio-Rad, Richmond, CA, USA) modifying the
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