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Interactions with lectins

Lectins, glycoproteins known for their ability to agglutinate erythrocytes in vitro, are present in many types of plants, including beans. Some lectins are toxic. Lectins interact with certain carbohydrates in a specific way. Lectins are still being studied. It appears that lectins may be involved in recognition between... [Pg.44]

Fig. 4 Enthalpy-entropy plot obtained by ITC measurement on a family of related microbial lectins interacting with natural and synthetic carbohydrates. Fig. 4 Enthalpy-entropy plot obtained by ITC measurement on a family of related microbial lectins interacting with natural and synthetic carbohydrates.
It has now been established that the BS II lectin interacts with the same determinant in blood-group substances derived from hog and human stomach linings as con A (see Section II, 1, j), namely, nonreducing, terminal 2-acetamido-2-deoxy-a-D-glucopyranosyl groups.4713... [Pg.208]

Theoretical aspects of affinity electrophoresis have been discussed and the applicability of the technique for determination of dissociation constants of protein-ligand complexes demonstrated. The pH dependence of lectin interactions with sugars has been determined by affinity electrophoresis. Association constants of dextrans and isomaltose oligosaccharides for myeloma anti-dextran have been determined using the technique. [Pg.590]

FIGURE 14.12 Computer-aided models of lectin interaction with glycoporphyrins functionalized S WCNT (above) and chemically converted graphene. (Adapted and reprinted from Ref. [246] with permission of American Chemical Society. Copyright 2012.)... [Pg.494]

A lectin, isolated from the seeds of Amphicarpaea bracteata by affinity chromatography on 2-acetamido-2-deoxy-D-galactose coupled to epoxy-activated agarose, has been shown to have characteristics common with Dolichos biflorus lectin, especially in relation to the agglutination of human Ai erythrocytes. It is assumed that the lectin interacts with non-reducing terminal 2-acetamido-2-deoxy-D-galactosyl residues on the red cell membrane of these erythrocytes. [Pg.304]

Study of lectin interaction with cell-siuface 257... [Pg.558]

The ability of PO to interact with the acetyl residues of chitin allows us to compare them with monovalent lectins (i.e. extensins) which when binding with hemicellulose are only affected in a medium with a high ionic strength (Brownleader et al., 2006). As a rule, POs are bound with the plant cell wall and act as its modifiers. Some POs can form complexes with an extensin of cell walls (Brownleader et al., 2006). Consequently, chitin-specific sites that are capable of interacting with polysaccharides exist in the molecules of PO, and these sites can resemble the membrane receptor binding sites or else be similar to the domains of heparinbinding proteins (Kim et al., 2001). [Pg.212]

Interact with specific carbohydrates Lectins, selectins (cell adhesion lectins), antibodies... [Pg.515]

After assessing the interesting optical properties of the complexes, specific protein interactions with ConA as a model lectin were investigated in preliminary... [Pg.278]


See other pages where Interactions with lectins is mentioned: [Pg.216]    [Pg.444]    [Pg.143]    [Pg.269]    [Pg.2447]    [Pg.439]    [Pg.476]    [Pg.647]    [Pg.685]    [Pg.654]    [Pg.12]    [Pg.533]    [Pg.1643]    [Pg.216]    [Pg.444]    [Pg.143]    [Pg.269]    [Pg.2447]    [Pg.439]    [Pg.476]    [Pg.647]    [Pg.685]    [Pg.654]    [Pg.12]    [Pg.533]    [Pg.1643]    [Pg.71]    [Pg.25]    [Pg.168]    [Pg.532]    [Pg.270]    [Pg.329]    [Pg.93]    [Pg.182]    [Pg.191]    [Pg.140]    [Pg.144]    [Pg.211]    [Pg.142]    [Pg.143]    [Pg.156]    [Pg.157]    [Pg.177]    [Pg.187]    [Pg.203]    [Pg.235]    [Pg.255]    [Pg.260]    [Pg.303]    [Pg.340]    [Pg.341]   
See also in sourсe #XX -- [ Pg.35 , Pg.180 ]




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