نتایج جستجو برای: binding lectin
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Snake venoms are complex mixtures of biologically active proteins and peptides. Many affect haemostasis by activating or inhibiting coagulant factors or platelets, or by disrupting endothelium. Snake venom components are classified into various families, such as serine proteases, metalloproteinases, C-type lectin-like proteins, disintegrins and phospholipases. Snake venom C-type lectin-like pro...
8-Azidoadenine was employed as a photoaffinity probe of the adenine binding site of the seed lectin from lima beans and from Phaseolus vulgaris erythroagglutinin. This compound was shown to (a) bind competitively to the adenine binding site of these lectins and (b) exhibit enhanced binding in the presence of 1,8-anilinonaphthalenesulfonic acid in the same manner as adenine. The presence or abse...
W. Mark ABBOTT,* Andrew MELLOR,t Yvonne EDWARDS$ and Ten FEIZI*§ *Section of Glycoconjugate Research, M.R.C. Clinical Research Centre, Watford Road, Harrow, Middx. HAl 3UJ, tDivision of Immunology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, and TMRC Human Biochemical Genetics Unit, The Galton Laboratory, University College London, Wolfson House, 4 Stephens...
L&in-induced agglutination is a complex process determined by several factprs such as the nature of lectin (valency, binding constant) the properties of cell membrane (fluidity, distribution of lectin receptor sites) and the metabolic state of the cell (microvilli, microtubules, microfilament) [l-3] . In order to assess quantitatively the effect of each of these factors, one has to obtain the t...
Equilibrium dialysis studies on the binding of the blood group B-specific Bandeiraea simplicifolia lectin to methyl alpha-D-galactopyranoside demonstrated the existence of one carbohydrate binding site per subunit for the tetrameric protein, with an intrinsic association constant of 8.6 x 10(4) (M) (-1) at 2 degrees and 3.3 x 10(4) (M)(-1) at 20 degrees. These values correspond to a free energy...
BACKGROUND Lectins are a diverse group of carbohydrate-binding proteins exhibiting numerous biological activities and functions. METHODS Two-step serial carbohydrate affinity chromatography was used to isolate a lectin from the edible mushroom clouded agaric (Clitocybe nebularis). It was characterized biochemically, its gene and cDNA cloned and the deduced amino acid sequence analyzed. Its ac...
Selectins are adhesion molecules that resist large tensile forces applied by hydrodynamic forces to leukocytes binding to vessel walls. In crystals, the liganded (high-affinity) and unliganded (low-affinity) conformations differ in orientation between their tandem lectin and EGF domains. I examine how tensile force exerted on a selectin-ligand complex in vivo could favor the more extended, high...
Incubation of PC12 cells preloaded with 125I-nerve growth factor (NGF) reveals rapidly and slowly dissociating binding components indicative of a heterogeneous population of receptors. If the cells are previously exposed to wheat germ agglutinin (WGA) for 30 min, NGF now binds to an apparently homogeneous receptor population which exhibit slow dissociation kinetics. Total binding is also reduce...
The endogenous beta-D-galactoside-binding lectins of UV-2237-IP3 fibrosarcoma cells consist of two polypeptides with molecular weights of 14,500 (L-14.5) and 34,000 (L-34). Recently we constructed complementary DNA (cDNA) libraries from these cells in the expression vector lambda gt11 and isolated and characterized cDNA clones encoding the two lectin species (A. Raz et al., Exp. Cell Res., 173:...
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