Please use this identifier to cite or link to this item: http://dspace.sctimst.ac.in/jspui/handle/123456789/80
Title: AFFINITY CHROMATOGRAPHIC ISOLATION OF CELL-SURFACE GLYCOPROTEINS FROM HUMAN FETAL BRAINS AND THEIR INTERACTION WITH LECTINS
Authors: ZACHARIAH, B
MARIKAR, Y
BASU, D
Keywords: Biochemistry
Issue Date: 1991
Publisher: INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS
Citation: INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS. 28; 41035; 412-417
Abstract: The cell surface glycoproteins of foetal human neurons and glial cells were isolated by affinity chromatography on Con A-Sepharose 4B. Dissociation of Con A from the matrix took place independent of buffer composition and the absence of lipids and/or detergents during chromatography. It was apparently related to the nature of glyco proteins. Pretreatment of Con A-Sepharose 4B with urea or guanidine minimized this problem. The elution of glycoproteins from the affinity matrix at 4-degrees-C, instead of the usual 25-degrees-C, reduced both Con A and glycolipid contamination in the eluate. Dot-enzyme-linked-lectin assay was carried out with horse radish peroxidase conjugated lectins and serotonin. It was observed that total glycoproteins contained high mannose, hybrid and a limited quantity of biantennary complex type oligosaccharide chains. O-linked oligosaccharides were also present. Desialylation and sodium chloride inhibited binding to serotonin and wheat germ agglutinin indicating the presence of sialic acid residues. Fucose was attached to the innermost core GlcNAc residue, as revealed by affinity towards pea lectin.
URI: http://dspace.sctimst.ac.in/jspui/handle/123456789/80
Appears in Collections:Journal Articles

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