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Glycoproteins interaction with concanavalin

Fig. I. Core structures of the carbohydrate units of nervous tissue glycoproteins. The structures are based on analytical data on rat brain glycoproteins and on assumptions of structural similarity with glycan cores from other sources. The main positions of variable or incomplete glycosylation are indicated by arrows. The approximate molar proportions of the glycans in rat brain and the mode of interaction with concanavalin A-Sepharose are indicated (the bisecting GicNAc residue affects the interaction of the diantennary glycans with concanavalin A) [9]. Fig. I. Core structures of the carbohydrate units of nervous tissue glycoproteins. The structures are based on analytical data on rat brain glycoproteins and on assumptions of structural similarity with glycan cores from other sources. The main positions of variable or incomplete glycosylation are indicated by arrows. The approximate molar proportions of the glycans in rat brain and the mode of interaction with concanavalin A-Sepharose are indicated (the bisecting GicNAc residue affects the interaction of the diantennary glycans with concanavalin A) [9].
Alkaline Phosphatases.—Since an alkaline phosphatase from Dictyostelium discoideum interacted with concanavalin A, it appears to be a glycoprotein. ... [Pg.424]

A single passage of a crude extract of human placenta through a column of concanavalin A immobilized on macroporous agarose effected the purification of an a-D-mannosidase by 300-fold. The nature of the interaction with concanavalin A indicated that the a-D-mannosidase is a glycoprotein. [Pg.350]

Western blotting has become an important, modern technique for analysis and characterization of proteins. The procedure consists of, first, the electrophoretic transfer (blotting) of proteins from polyacrylamide gels to synthetic membranes. The transferred blots are then probed using immunological detection methods to identify proteins of specific structure and/or function. In this experiment, bovine serum will be fractionated by SDS-PAGE and the proteins blotted onto a nitrocellulose membrane. Serum glycoproteins will be identified by their specific interaction with the lectin concanavalin A. [Pg.321]

Surolia A, Bishayee S, Ahmad A, Balasubramanian KA, Thambi-Dorai D, Poddar SK, Bacchawat BK (1975) Studies on the interaction of concanavalin A with glycoproteins. In Chowdhuri TK, Weiss AK (eds) Concanavalin A. Plenum Press, New York, London, p 95... [Pg.225]

Nucieotidases.—Since the 5 -nucleotidase from Dictyostelium discoideum interacted with immobilized concanavalin A, it appears to be a glycoprotein. Pectinesterases.—The occurrence, formation, assay, purification, and specificities of pectinesterases have been reviewed. Pectinesterase activity was detected both in healthy and diseased onions Allium cepa), but not in cultures of the invading bacterium (Pseudomonas cepacia) Both the pectinesterase and poly-D-galact-uronate lyase activities of Clostridium multifermentans are associated with a single complex. ... [Pg.426]

Concanavalin A (continued) Studies of the interaction of concanavalin A with Trypanosoma equiperdum and isolation of the antigenic glycoprotein 104... [Pg.456]

A direct method involving fluorescent-light microscopy and sodium dodecyl sulphate gel electrophoresis has been developed for the study of the binding of lectins to glycoproteins and subunits thereof. Fluorescein-labelled concanavalin A was shown to interact with both agglutinins (RCAI and RCAII) from Ricinus communis, rather than with RCAI only as suggested by other reports. [Pg.297]

The glycocalyx (cell coat) of Ehrlich ascites tumour cells, which is rich in glycoproteins and glycosaminoglycans, contains only one fraction (mol. wt. 1.3 X 10 ) which interacts with I-concanavalin A. ... [Pg.333]

Studies of the binding of glycoproteins in microsomal and Golgi membranes to lectins Studies of the interactions of Mucor sp. acid proteases with concanavalin A Affinity chromatography of serum proteins ... [Pg.529]

The reactions of glucose containing a SAM with the lectin, concanavalin A, has been reported (29). This large protein complex interacts specifically with terminal D-glucose and D-mannose sugars that are frequently incorporated on complex glycoproteins which function as cell surface receptors and in transmembrane... [Pg.108]

Removal of polysaccharide contaminants from preparations of DNA by affinity chromatography Separation of membrane glycoproteins from rat-brain synaptic vesicles by affinity chromatography Studies of the interactions of the carbohydrate-binding sites on concanavalin A with adipocyte receptors... [Pg.529]

See other pages where Glycoproteins interaction with concanavalin is mentioned: [Pg.271]    [Pg.310]    [Pg.291]    [Pg.343]    [Pg.11]    [Pg.368]    [Pg.166]    [Pg.7]    [Pg.242]    [Pg.150]    [Pg.177]    [Pg.215]    [Pg.592]    [Pg.593]    [Pg.8]    [Pg.389]    [Pg.1135]    [Pg.6]    [Pg.251]    [Pg.53]    [Pg.290]    [Pg.338]    [Pg.307]    [Pg.340]    [Pg.282]    [Pg.142]    [Pg.56]    [Pg.300]    [Pg.516]    [Pg.331]    [Pg.371]    [Pg.277]    [Pg.158]    [Pg.308]    [Pg.313]    [Pg.183]   
See also in sourсe #XX -- [ Pg.177 , Pg.178 ]



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Concanavalin

Interaction with concanavalin

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