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

for comparison. Previous data (Tulp et al.,33 Conti et al.34) shows that the difference between the isoelectric points (pI) between the phenotypes βLG A and βLG B is only 0.3 pH unit. Figure 3 shows that bovine βLG A/B focused into two bands with pIs of 5.1 and 5.3. Peak I (fractions 3543) has the same pI as phenotype βLG A (5.3), and peak II (fractions 4755) has the same pI as phenotype βLG B (5.1).


Conclusions
We have developed a novel method for purifying and separating bovine βLG A and B variants by preparative electrophoresis. The molecular weight and the isoelectric points of the eluted peak 1 (fractions 3543) and the eluted peak 2 (fractions 4755) separated by continuous electrophoresis, were analyzed by analytical SDS-PAGE and IEF. Since the molecular weight and the isoelectric points of peak 1 were the same as those of βLG A, and the molecular weight and the isoelectric point of fraction II the same as those of bovine βLG B, we suggest that the eluted fraction I and the eluted fraction II are bovine βLG A and B variants, respectively. Both fractions were recognized with antiserum to bovine βLG A/B. The molecular weight and isoelectric points of other milk proteins, used as controls, were different from those of the eluted fractions and were not recognized by antiserum to bovine βLG (data not shown). The results confirm that the two eluted fractions are specific βLG phenotypes and do not contain any impurities. The method could be used both in analytical and preparative scale in milk industry and when studying bovine milk allergy.


References
1. Conti,
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