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Tabun binding

Tabun-inhibited enzyme (an O-ethyl N,N-dimethylamidophosphoro derivative) is slow to reactivate and Heilbronn (1963) found no detectable spontaneous reactivation with human acetylcholinesterase. The reasons for this are becoming more clear. Tabun binding of mouse acetylcholinesterase causes conformational changes in the enzyme that may stabilize the enzyme-inhibitor complex even without ageing of the complex (Ekstrom et al., 2006). [Pg.200]

It was shown that tabun, sarin, soman, and VX bind to the muscarinic receptor subtype m2, leading to the assumption... [Pg.771]

While the biological role of ChE is presently unelear, it is known that soman, sarin, tabun, and VX bind to ChE, without any apparent toxic effects, decreasing the amount of free agents available for inhibition of AChE in the eentral nervous system and erythrocytes. Pretreatment with human... [Pg.803]

It binds to the enzyme and destroy the active site, or otherwise screw the protein. Suicide inhibitors, a special class of such inhibitors, are activated by the normal catalytic activity of the enzyme, but form an intermediate that binds to and destroys the active site. Irreversible inhibitors bind tightly (often covalently) to the enzyme and cannot be removed by dialysis. They include such things as nerve gases (Sarin, DIPF, Tabun) and insecticides (Malathion). [Pg.193]

FIGURE 19.1 Chemical structures of nerve agents the nerve agents sarin (GB), soman (GD), and cyclosarin (GF) lose fluorine subsequent to binding to cholinesterase. The agents tabun (GA), VX, and Russian VX lose CN, and the thiol groups, respectively. [Pg.505]

H]L-PIA) to the brain membranes in a dose-dependent manner. Soman was fonnd to be five and nine times more effective than tabun and sarin, respectively, in inhibiting [ H]L-PIA binding. They snggested that nerve agents could interact directly at the A1 adenosine receptors, which could subsequently mediate changes in permeability of the synaptic membrane, with possible effects on Na and/or Ca conductance. [Pg.119]

Tyrosine adducts were found in guinea pigs and marmosets poisoned with sarin, soman, cyclosarin, and tabun. VX, which is less reactive than other WNAs, formed an adduct in human plasma in vitro only at high concentrations (Williams et al., 2007 Black, 2010 Black and Read, 2013). Tyrosine adducts were less sensitive than ChE as biomarkers with respect to exposure levels but were more stable and did not undergo an aging reaction such as OP binding to serine esterases (Read et al.,... [Pg.892]


See other pages where Tabun binding is mentioned: [Pg.278]    [Pg.442]    [Pg.487]    [Pg.25]    [Pg.701]    [Pg.763]    [Pg.799]    [Pg.805]    [Pg.806]    [Pg.807]    [Pg.91]    [Pg.127]    [Pg.13]    [Pg.15]    [Pg.30]    [Pg.698]    [Pg.198]    [Pg.231]    [Pg.260]    [Pg.141]    [Pg.142]    [Pg.287]    [Pg.76]    [Pg.118]    [Pg.825]    [Pg.90]    [Pg.237]    [Pg.611]    [Pg.502]    [Pg.186]    [Pg.27]    [Pg.553]    [Pg.102]    [Pg.593]    [Pg.835]    [Pg.836]    [Pg.884]    [Pg.888]    [Pg.890]    [Pg.892]    [Pg.87]   
See also in sourсe #XX -- [ Pg.237 ]




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