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  1. Home
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Browsing by Author "BASU, D"

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    A GALACTOMANNAN-HYDROLYZING ALPHA-GALACTOSIDASE FROM JACK FRUIT (ARTOCARPUS-INTEGRIFOLIA) SEED - AFFINITY CHROMATOGRAPHIC PURIFICATION AND PROPERTIES
    (JOURNAL OF BIOSCIENCES, 1987) APPUKUTTAN, PS; BASU, D
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    AFFINITY CHROMATOGRAPHIC ISOLATION OF CELL-SURFACE GLYCOPROTEINS FROM HUMAN FETAL BRAINS AND THEIR INTERACTION WITH LECTINS
    (INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS, 1991)
    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.
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    ALPHA-GALACTOSIDE-BINDING ISOLECTINS FROM WILD JACK FRUIT SEED (ARTOCARPUS-HIRSUTA) - PURIFICATION AND PROPERTIES
    (INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS, 1989) ANTONY, L; BASU, D; APPUKUTTAN, PS
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    CHARACTERIZATION OF CONCANAVALIN-A-BINDING-NEURONAL AND GLIAL SURFACE GLYCOPROTEINS FROM HUMAN FETAL BRAIN
    (INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS, 1992)
    Neuronal and glial surface glycoproteins have been isolated from human foetal brains by affinity chromatography on 8 M urea or 6 M guanidine-treated Con A-Sepharose 4B at 4-degrees-C and three groups of glycoproteins of molecular mass 65-73 kDa, 52-63 kDa and 43-48 kDa have been identified on SDS/PAGE. These glycoproteins exhibited anomalous behaviour on SDS/PAGE, indicating the existence of a gradation of mutually interconvertible protein-SDS aggregates in dynamic equilibrium with one another. Deglycosylation and deacylation did not alter the SDS/PAGE multiple band pattern. Purified glycoproteins contained 160 +/- 90-mu-g carbohydrate/mg protein, and a sialic acid content of 25 +/- 5 nmole/mg protein. The N-terminals were blocked. The glycoproteins moved preferentially on acid/urea/PAGE. Sepharose 6B gel filtration in the absence of lipid and detergents resolved the glycoproteins into an excluded peak I and a low molecular mass peak II. Peaks I and II were non-interconvertible on Sepharose 6B gel filtration or on reversed phase HPLC in an isopropanol/water/TFA gradient system. Both peaks rendered a single fast moving band of identical mobility on acid/urea/PAGE, suggesting that peak I was possibly a micellar aggregate of the monomeric peak II. The glycoproteins were refractory to digestion by trypsin or pronase and reacted identically towards various lectins. Attempts to raise antibodies in rabbit against the isolated glycoproteins were unsuccessful. The physicochemical properties apparently reflect an inherent tendency of these glycoproteins to form self aggregates, a characteristic of amphipathic membrane proteins.
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    CHARACTERIZATION OF LYSOSOMAL ALPHA-MANNOSIDASE FROM HUMAN-PLACENTA
    (INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS, 1988) BASU, D; NAIR, J; KHAN, FA
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    HUMAN BRAIN CREATINE-KINASE BINDING TO IMMOBILIZED CIBACRON BLUE F3GA - CHARACTERIZATION AND USE IN PURIFICATION OF THE ENZYME
    (INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS, 1992)
    Creatine kinase (ATP: creatine N-phosphotransferase, EC 2.7.3.2) from adult human brain grey matter was purified by cibacron blue F3GA-Sepharose affinity chromatography. By gel electrophoresis of the purified enzyme under non-denaturing conditions a single protein band was observed. The dye-bound enzyme was eluted using its substrate, ATP. Reversibility of the binding of purified creatine kinase to blue Sepharose by ATP in a concentration-dependent manner indicated that the cibacron blue molecule which structurally mimics nucleotides occupied the substrate binding site of the enzyme. Also the marked dependence of enzyme binding to blue Sepharose on Mg2+ concentration suggested that Mg2+ ion is capable of combining with the dye moiety to form a site-specific binding complex that is similar to the physiological substrate of creatine kinase, namely Mg2+-ATP or Mg2+-ADP.
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    LEACHING OF CONCANAVALIN-A DURING AFFINITY CHROMATOGRAPHIC ISOLATION OF CELL-SURFACE GLYCOPROTEINS FROM HUMAN FETAL NEURONS AND GLIAL-CELLS
    (ANALYTICAL BIOCHEMISTRY, 1992)
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    OLIGOSACCHARIDE STRUCTURE DETERMINATION OF GLYCOCONJUGATES USING LECTINS
    (JOURNAL OF BIOSCIENCES, 1987) BASU, D; NAIR, JV; APPUKUTTAN, PS
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    PHYSICOCHEMICAL PROPERTIES AND BINDING-SITE AMINO-ACID-RESIDUES OF GALACTOSIDE-BINDING PROTEIN OF HUMAN-PLACENTA
    (JOURNAL OF BIOSCIENCES, 1987) NAMBIAR, MP; BASU, D; APPUKUTTAN, PS
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    PRELIMINARY CRYSTALLOGRAPHIC STUDY OF THE ALPHA-D-GALACTOSE-SPECIFIC LECTIN FROM JACK FRUIT (ARTOCARPUS-INTEGRA) SEEDS
    (JOURNAL OF MOLECULAR BIOLOGY, 1988)
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    SURFACE CARBOHYDRATES IN CELL-SOCIOLOGY
    (INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS, 1993)
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