The Purification of Soybean 11S Globulin with ConA-Sepharose 4B and Sepharose 6B
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Coupling of glycosaminoglycans to agarose beads (sepharose 4B).
1. Heparin, heparan sulphate, chondroitin sulphate and dermatan sulphate were covalently attached to beads of agarose activated by cyanogen bromide. The bond is probably mediated by the amino group of a serine or peptide residue at the reducing end of the polysaccharide chain. 2. The uptake of glycosaminoglycan during the coupling procedure is about 0.9mg/ml of wet gel. However, direct analysis...
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1. The isolation of transferrin from rat serum by means of affinity chromatography on CNBr-activated Sepharose 4 B is described. -2. Subfractionation by isoelectric focusing yielded two transferrin fractions with identical biological behaviour but with small differences in isoelectric point (6.0 and 5.8) and sialic acid contents.
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The sorting determinants of glycinin, a soybean (Glycine max) 11S globulin, which mediates protein targeting to the protein storage vacuole (PSV), were investigated in maturing soybean cotyledons by transient expression assays. A C-terminal stretch of 10 amino acids of A1aB1b, a glycinin group I subunit, was sufficient to direct green fluorescent protein (GFP) to the PSV. This peptide may corre...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1974
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.38.1083