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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

Evaluation of standardized ileal digestible lysine requirement of nursery pigs from seven to fourteen kilograms.

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Four experiments were conducted to determine the standardized ileal digestible (SID) Lys requirement of pigs (Sus scrofa) from 7 to 14 kg. In Exp. 1, 294 pigs (6.8 kg BW) were used in a 28-d growth trial with 7 pigs per pen and 7 pens per treatment. Treatment diets were fed from d 0 to 14, and a

Detection of lectins in nodulated peanut and soybean plants.

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The direct double-antibody enzymelinked immunosorbent assay system was used in the detection and measurement of seed lectins from peanut (Arachis hypogaea L.) and soybean (Glycine max L.) plants (PSL and SBL, respectively) that had been inoculated with their respective rhizobia. Concentrations of

Influence of media composition on the production of delta-endotoxin by Bacillus thuringiensis var. thuringiensis.

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Powders of edible leguminous seeds, greengram (Vigna radiata) or soybean (Glycine max), were used as the major protein source with different combinations of soluble starch and/or cane sugar molasses as the major carbohydrate source for the production of delta-endotoxin by Bacillus thuringiensis var.

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

A possible mechanism for the cellular coaggregation between Actinomyces viscosus ATCC 19246 and Streptococcus sanguis ATCC 10557.

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The cells of Actinomyces viscosus ATCC 19246 (Av19246) and Streptococcus sanguis ATCC 10557 (Ss10557) coaggregated immediately after mixing in 40 mM-Tris/HCl buffer. Optimal conditions were pH 7.5 in the presence of Ca2+ at 0.1 mM or higher. Na2 EDTA and its analogues, Na2MgEDTA and Na2MnEDTA at 7.5

Characterization of alpha-mannosidase from Erythrina indica seeds and influence of endogenous lectin on its activity.

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alpha-mannosidase from Erythrina indica seeds is a Zn(2+) dependent glycoprotein with 8.6% carbohydrate. The enzyme has a temperature optimum of 50 degrees C and energy of activation calculated from Arrhenius plot was found to be 23 kJ mol(-1). N-terminal sequence up to five amino acid residues was

Biochemical and immunological properties of alkaline invertase isolated from sprouting soybean hypocotyls.

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Alkaline invertase from sprouting soybean (Glycine max) hypocotyls was purified to apparent electrophoretic homogeneity by consecutive use of DEAE-cellulose, green 19 dye, and Cibacron blue 3GA dye affinity chromatography. This protocol produced about a 100-fold purification with about a 11% yield.

Epitope Ligand Binding Sites of Blood Group Oligosaccharides in Lectins Revealed by Pressure-Assisted Proteolytic Excision Affinity Mass Spectrometry.

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Affinity mass spectrometry using selective proteolytic excision and extraction combined with MALDI and ESI mass spectrometry has been applied to the identification of epitope binding sites of lactose, GalNac, and blood group oligosaccharides in two blood group-specific lectins, human galectin-3 and

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