Lectins receptor

Many other capture molecules could also be used (e.g., receptors, lectins) the principles of such methods do not differ from those discussed here. 

For every protein purification problem there is always an affinity solution, but cost and safety considerations may render these solutions impractical. As an example, antibodies are widely used for analysis, where only relatively small amounts are usually required, but their production and purification on a large scale for preparative-scale chromatography may be difficult to justify economically. In some cases, Hhybridoma technology may be able to address this problem. Even if production costs are acceptable, the immobilized antibodies may be unstable over the sequence of sample application, elution, and sanitation required for multiple use of the affinity adsorbent. For these reasons, while biological ligands (antibodies, enzymes, receptors, lectin. 

C, which is found in complement proteins FI, F2, and F3, first found in fibronectin I, the immunoglobulin superfamily domain N, found in some growth factor receptors E, a module homologous to the calcium-binding E-F hand domain and LB, a lectin module found in some cell surface proteins. (Adapted from Baron, M., Norman, D., and Campbell, I., 1991, Protein modnles. Trends in Biochemical Sciences 16 13—1 7.)... 

Concanavalin A is a plant lectin from the jack bean (Canavalia ensiformis) which binds with high affinity to mannose residues of glycoproteins. Concanavalin A is known to stimulate the tyrosine kinase activity of the INSR (3-subunit with consecutive activation of kinases downstream the insulin receptor (IRS, PI 3-kinase). It is believed that Concanavalin A stimulates the activation and autophosphorylation of the INSR kinase through aggregation of the receptor, although the precise mechanism of action is unclear. 

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). 

Binding proteins such as antibodies, receptors, and lectins may spontaneously aggregate in presence of bi- or multivalent specific ligands. This process, however, often results in assemblies that lack well-defined morphological and structural elements. 

C-type lectins Characterized by a Ca +-dependent carbohydrate recognition domain (CRD) includes the mammalian asialoglycoprotein receptor, the selectins, and the mannosebinding protein... 

Glycophorin A appears to serve a variety of functions on the red-cell membrane, and has been implicated in several red-cell disorders. Because it extends from the external environment of the cell into the cell cytoplasm, it is considered to constitute a receptor for malarial parasites,"" influenza viruses, lectins, and Portuguese man-of-war toxin. Many of these receptor functions are attributable to the carbohydrate composition of these... 

Douglas SD (2001) Methadone may promote HIV replication study. AIDS Alert 16 120 Dreyer EB, Kaiser PK, Offermann IT, Lipton SA (1990) HIV-1 coat protein neurotoxicity prevented by calcium channel antagonists. Science 248 364-367 Dunn S, Vohra RS, Murphy JE, Homer-Vanniasinkam S, Walker JH, Ponnambalam S (2008) The lectin-like oxidized low-density-lipoprotein receptor a pro-inflammatory factor in vascular disease. Biochem J 409 349-355... 

JORDINSON M, DEPREZ P H, PLAYFORD R J, HEAL S, FREEMAN T 0, ALISON M, CALAM J (1996) Soybean lectin stimulates pancreatic exocrine secretion via CCK-A receptors in rats. Am J Physiol. 270 G653-9. 

PUSZTAI A, EWEN S W, GRANT G, PEUMANS W J, VAN DAMME E J, COATES M E, BARDOCZ S (1995) Lectins and also bacteria modify the glycosylation of gut surface receptors in the rat Glycoconj J. 12 22-35. 

This process seems to reflect gradual increases in the intensity and density of labelled receptor cell bodies and their axons, followed by regional bulbar staining as synaptogenesis proceeds. However, a more extensive range of lectins needs to be examined before the implications of species differences in the membrane glycoproteins can be satisfactorily interpreted (Salazar and Quinteiro, 1998). 

An intriguing possibility is that the IDGFs could interact as lectins with the insulin receptor itself, which is already known to bind other lectins. Wheat germ... 

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