Abstract
β-conglutin from Lupinus campestris was extracted and purified by gel filtration chromatography. The protein with molecular mass around 190 kDa showed by SDS-PAGE three major polypeptides of 53, 60 and 63 kDa and a minor polypeptide of 30 kDa. Isoelectric focusing of the native protein gave three isoforms with isoelectric points of 6.2, 6.3 and 6.4. Its sedimentation coefficient was 8.0S, with a hydrodynamic diameter of 110 Å and possessed antigenic determinants in common with 7S proteins from common bean and soybean.
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