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- Title
A PROCEDURE FOR THE PURIFICATION OF BETA-LACTOGLOBULIN FROM BOVINE MILK USING GEL FILTRATION CHROMATOGRAPHY AT LOW pH.
- Authors
Naqvi, Zainab; Khan, RizwanHasan; Saleemuddin, Mohammed
- Abstract
A simple and rapid procedure for the purification of beta-lactoglobulin (β-LG) from bovine milk is described. The procedure exploits the major difference in molecular mass of β-LG and other whey components and the existence of the former in monomeric form at acidic pH. Gel filtration of whey was carried out using a Bio-Gel P10 column at pH 3.0. Residual caseins and other milk proteins were excluded from the gel and β-LG and alpha-lactalbumin (α-LA) emerged as two fully resolved peaks. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) suggested that β-LG was purified to apparent homogeneity, while absorption, fluorescence, and circular dichroism spectroscopy indicated the native-like conformation of the protein. Western blot analysis revealed that the antibodies raised against the purified β-LG in rabbits also readily react with the commercial bovine protein. This procedure requires only 4-5 hr for the purification of about 10 mg of β-LG from a single run while using a small column (2.3 cm × 83 cm) of Bio-Gel P10 and has the potential for scaling up.
- Subjects
LACTOGLOBULINS; GELATION; MILK; WHEY; EUROPEAN rabbit; POLYACRYLAMIDE gel electrophoresis
- Publication
Preparative Biochemistry & Biotechnology, 2010, Vol 40, Issue 4, p326
- ISSN
1082-6068
- Publication type
Academic Journal
- DOI
10.1080/10826068.2010.525405