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Purification of melibiose-binding lectins from two cultivars of Chinese black soybeans.
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A dimeric 50 kDa melibiose-binding lectin was isolated from the seeds of the cultivar of soybean (Glycine max), called the small glossy black soybean. The isolation procedure comprised ion exchange chromatography on Q Sepharose, SP Sepharose and Mono Q followed by gel filtration on Superdex 75. The
Biochemical and functional properties of a lectin purified from korean large black soybeans--a cultivar of glycine max.
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Lectins, a class of proteins that reversibly and non-enzymatically bind specific sugars, have been purified from different kinds of legumes. In this study, a 48-kDa lectin (KBL) was purified from Korean large black soybeans using liquid chromatography. The specific hemagglutinating activity of the
Separation of disaccharides by affinity capillary electrophoresis in lectin-containing electrophoretic solutions.
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Separation of the 1-phenyl-3-methyl-5-pyrazolone (PMP) derivatives of simple disaccharides (maltose, cellobiose, gentiobiose, lactose, and melibiose) by affinity capillary electrophoresis was investigated using lectin-containing neutral phosphate buffers, filled in a linear polyacrylamide-coated
Ion exchange and affinity chromatography in the scaleup of the purification of alpha-galactosidase from soybean seeds.
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Soybeans (Glycine max) contain an alpha-galactosidase that makes up a small fraction of the total protein of the seed. The properties of this enzyme are of interest because of its potential to convert the galactooligosaccharides, stachyose and raffinose, in soybean meal to sugars digestible in the
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