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1 atment with the histidine-modifying compound diethylpyrocarbonate.
2 tive to N-ethylmaleimide, phenylglyoxal, and diethylpyrocarbonate.
3 activated by the histidine-modifying reagent diethylpyrocarbonate.
4 with RNases T1 and V1 and the small molecule diethylpyrocarbonate.
5 form, and hypochlorite but more resistant to diethylpyrocarbonate.
6 different covalent labeling reagents, namely diethylpyrocarbonate, 2,3-butanedione, and the reagent p
7 is finding contradicts earlier results using diethylpyrocarbonate alone, which suggested an RNA synth
8 r clearance by using potassium permanganate, diethylpyrocarbonate and methidiumpropylEDTA.Fe(II) foot
10 oscopy, histidine modification studies using diethylpyrocarbonate, and enzymatic activity measurement
11 to N-ethylmaleimide, F-, phenylglyoxal, and diethylpyrocarbonate, both substrates appear to be hydro
12 it was shown that both histidines react with diethylpyrocarbonate but that only reaction with His-8 r
13 by quinine, Gd3+, La3+ and the His modifier diethylpyrocarbonate, but not by the Ca2+ or K+ channel
14 me A (OSB-CoA) synthetase, when treated with diethylpyrocarbonate (DEP), showed a time-dependent loss
15 studies involving chemical modification with diethylpyrocarbonate (DEPC) and site-directed mutagenesi
16 The reliability and information content of diethylpyrocarbonate (DEPC) as a covalent probe of prote
17 ication of histidyl residues of tubulin with diethylpyrocarbonate (DEPC) at a mole ratio of 0.74 (DEP
18 yme, H61A, H62A, and H79A, and the effect of diethylpyrocarbonate (DEPC) have been investigated to el
19 In this work, we describe a method that uses diethylpyrocarbonate (DEPC) labeling and mass spectromet
20 Experiments with the His-specific reagent diethylpyrocarbonate (DEPC) showed that one or more His
23 ibitory binding site was also assessed using diethylpyrocarbonate (DEPC), which modifies histidines.
27 nate (CMCT; to probe U at N-3 and G at N-1), diethylpyrocarbonate (DEPC; to probe A at N-7), dimethyl
29 estored 95% activity, results that indicated diethylpyrocarbonate inactivates the enzyme by the speci
30 thanosarcina thermophila was investigated by diethylpyrocarbonate inactivation and site-directed muta
35 ase reaction was suggested by the ability of diethylpyrocarbonate to block formation of mevalonate fr
36 ivity of zinc potentiation of alpha4beta4 to diethylpyrocarbonate treatment and alterations in pH sug
37 H:FR activities in a reversible manner while diethylpyrocarbonate treatment resulted in complete irre
39 nated with ribonuclease unless the inhibitor diethylpyrocarbonate was used during the ribonucleic aci
40 kinetics of inactivation of E. coli Lgt with diethylpyrocarbonate were consistent with the modificati
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