Purification and properties of a beta-galactoside-binding lectin from neonatal marmoset.
A beta-galactoside-binding lectin was extracted from whole neonatal marmoset homogenate with lactose solution and purified to homogeneity by ion-exchange chromatography on Q Sepharose Fast Flow and by affinity adsorption to trypsinized and glutaraldehyde-fixed ghosts of rabbit erythrocytes. The lectin has a dimeric structure composed of two 15K subunits. Its amino acid composition and partial amino acid sequences were quite similar to those of beta-galactoside-binding lectins from human placenta and lung.
Pharmaceutical Research Laboratories, Meiji Seika Kaisha, Ltd., Kanagawa.
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Ohsawa
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Hirano
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Natori
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000831:Animals, Newborn / Q000378:metabolism*; D002143:Callitrichinae / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D037161:Galectins; D006386:Hemagglutination Tests; D006388:Hemagglutinins / Q000032:analysis / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D009005:Monosaccharides / Q000494:pharmacology; D013194:Staining and Labeling; D014357:Trypsin
D000596:Amino Acids; D037161:Galectins; D006388:Hemagglutinins; D009005:Monosaccharides; D014357:Trypsin