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MOLECULAR CHARACTERIZATION OF THE β‐CONGLUTIN OF LUPIN SEEDS
Author(s) -
MARTÍNEZAYALA ALMA LETICIA,
PAREDESLÓPEZ OCTAVIO
Publication year - 2001
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2001.tb00722.x
Subject(s) - size exclusion chromatography , isoelectric point , isoelectric focusing , molecular mass , chemistry , biochemistry , chromatography , gel permeation chromatography , biology , enzyme , organic chemistry , polymer
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.