نتایج جستجو برای: toxin binding
تعداد نتایج: 463901 فیلتر نتایج به سال:
Studies of the reaction of antibody A2B5 and tetanus toxin with pancreatic islet cells, islet cell tumors, and other human amine precursor uptake and decarboxylation (APUD) tumors are described. By indirect immunofluorescence, antibody A2B5 and tetanus toxin were shown to specifically bind to the plasma membrane of human, rat, chicken, and mouse islet cells. The binding of antibody A2B5 to the ...
The five B-subunits (CTB5) of the Vibrio cholerae (cholera) toxin can bind to the intestinal cell surface so the entire AB5 toxin can enter the cell. Simultaneous binding can occur on more than one of the monosialotetrahexosylganglioside (GM1) units present on the cell surface. Such simultaneous binding arising from the toxins multivalency is believed to enhance its affinity. Thus, blocking the...
We have studied the binding of alpha-bungarotoxin to a particulate fraction of goldfish brain enriched in synaptosomes. The binding is specific and saturable and exhibits the pharmacological properties of a nicotinic cholinergic receptor. Equilibrium binding measurements yield a single dissociation constant (KD) of 0.92 nM. Kinetic analysis revealed one association rate constant and two dissoci...
The molecular mechanisms of insect resistance to Cry toxins generated from the bacterium Bacillus thuringiensis (Bt) urgently need be elucidated enable improvement and sustainability Bt-based products. Although downregulation expression midgut receptor genes is a pivotal mechanism Bt toxins, underlying transcriptional regulation these remains elusive. Herein, we unraveled regulatory ABC transpo...
Binding properties of detergent-solubilized receptors for alpha-bungarotoxin from skeletal muscle of the 13th day chick embryo and from optic lobe of the hatching chick were compared. It was found that both types of receptor are nicotinic, although they differ in their affinities for individual ligands and in the rank order of ligands. In contrast to the muscle receptor, the neuronal receptor b...
Polypeptide neurotoxins alter ion channel gating by binding to extracellular receptor sites, even though the voltage sensors are in their S4 transmembrane segments. By analysis of sodium channel chimeras, a beta-scorpion toxin is shown here to negatively shift voltage dependence of activation and enhance closed state inactivation by binding to a receptor site that requires glycine 845 (Gly-845)...
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