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1                                              DEPC (1 mM) abolished Zn2+-induced inhibition and also t
2                                              DEPC and [(14)C]DEPC modification, coupled with amino ac
3                                              DEPC does not affect the absorption spectrum of cytochro
4                                              DEPC has a primary (18)O isotope effect of 1.041 +/- 0.0
5                                              DEPC modification indicates that the I state in Na(+)-in
6                                              DEPC was used to further characterize the inhibition bec
7 he histidines using nonradiolabeled and [14C]DEPC indicates that between one and two histidine residu
8                    Plasmin digestion of [14C]DEPC-treated Cp (and N-terminal sequence analysis of the
9                            Quantitative [14C]DEPC binding studies indicated the importance of a singl
10                           Labeling with [14C]DEPC localized both of these histidyl residues on beta-t
11 yrocarbonate (DEPC) at a mole ratio of 0.74 (DEPC/total His residues) for 3 min at 25 degreesC comple
12 ue, suggesting an active site location for a DEPC target.
13                                Additionally, DEPC-labeled histidine and lysine residues with higher r
14 oth A 5-P and PEP protect the mutant against DEPC inactivation but to different extents from those ob
15  The H97G mutant is protected by PEP against DEPC inactivation to the same degree as the wild-type en
16        The H241G mutant is protected against DEPC inactivation by PEP and A 5-P to the same extent as
17        KDO 8-P synthase is protected against DEPC inactivation by PEP and partially protected against
18  DAH 7-P synthase (Phe) is protected against DEPC inactivation by phosphoenolpyruvate, whereas d-eryt
19                           Protection against DEPC inactivation is afforded by a substrate analogue, s
20 on is first order with respect to enzyme and DEPC concentrations with a pseudo-second order rate cons
21 he inactivation is first-order in enzyme and DEPC.
22 fication studies using hydroxyl radicals and DEPC identify nonoverlapping primary binding sites for S
23 d in vitro and in vivo by using the SEPC and DEPC MRI approaches were well correlated (r (2) > 0.97),
24 llows the rank order POPC/POPG approximately DEPC/DEPG > DPePC/DPePG > DOPC/DOPG.
25 were carried out in explicit lipid bilayers (DEPC, POPC, DMPC, sphingomyelin), confirming the observe
26 at modification of His residues of band 3 by DEPC reduced I- quenching at pH 6.
27 h isoform E subunit are N-carbethoxylated by DEPC.
28                   H79 is also derivatized by DEPC at pH 7.0 and above, whereas H62 does not react at
29 4C]UDP-GlcUA uptake rates were diminished by DEPC treatment of intact microsomes, the accumulation of
30                     The inhibitory effect by DEPC was significantly protected (90%) by pretreating th
31 sts that the inactivation of heparinase I by DEPC is specific for histidine residues.
32 ts that the inactivation of heparinase II by DEPC is specific for histidine residues and that three h
33 At pH 6.5 wild-type enzyme is inactivated by DEPC after derivatization of one histidine, shown to be
34 econd order rate constant of inactivation by DEPC of 4.9 +/- 0.8 m(-1) s(-1) at pH 6.8 and 4 degrees
35 protects the cytochrome from inactivation by DEPC, indicating that the essential histidine is in the
36                           This inhibition by DEPC was also reversed by hydroxylamine.
37 hains (Ser, Thr, and Tyr) can be modified by DEPC in addition to other residues such as His, Lys, and
38 es and that three histidines are modified by DEPC.
39 hese two peptides did not become modified by DEPC.
40 ine and lysine residues had been modified by DEPC.
41 nterestingly, modification of the protein by DEPC was also found to reduce the metal cluster.
42 xyformylation of three histidine residues by DEPC.
43                              DEPC and [(14)C]DEPC modification, coupled with amino acid sequencing an
44          To test this hypothesis, we compare DEPC labeling reactivity of Ser, Thr, and Tyr residues i
45                       Under these conditions DEPC reacts only with histidyl residues.
46                        Diethylpyrocarbonate (DEPC) is a simple to use, commercially available covalen
47                        Diethylpyrocarbonate (DEPC) labeling analyzed with mass spectrometry can provi
48                        Diethylpyrocarbonate (DEPC) treatment of the protein abolished its binding to
49  at N-3 and G at N-1), diethylpyrocarbonate (DEPC; to probe A at N-7), dimethyl sulfate (DMS; to prob
50 ed carbonyl (ABUC) and diethylpyrocarbonate (DEPC), and insulin and beta2-microglobulin (beta2m) as m
51 chemically modified by diethylpyrocarbonate (DEPC).
52  study, we investigate diethylpyrocarbonate (DEPC) covalent labeling-mass spectrometry as a means of
53  study, we investigate diethylpyrocarbonate (DEPC) covalent labeling-mass spectrometry as a means of
54 ing when reagents like diethylpyrocarbonate (DEPC) are used for CL because of the differences in the
55 information content of diethylpyrocarbonate (DEPC) as a covalent probe of protein surface structure h
56 79A, and the effect of diethylpyrocarbonate (DEPC) have been investigated to elucidate the dehydratas
57 lfonic acid (DIDS), or diethylpyrocarbonate (DEPC).
58 e His-specific reagent diethylpyrocarbonate (DEPC) showed that one or more His residues was specifica
59 l modification reagent diethylpyrocarbonate (DEPC) was used to modify alpha 1-acid glycoprotein (oros
60 dine-modifying reagent diethylpyrocarbonate (DEPC).
61 y, we demonstrate that diethylpyrocarbonate (DEPC) covalent labeling mass spectrometry can provide bi
62   In this work, we use diethylpyrocarbonate (DEPC)-based covalent labeling together with LC-MS/MS ana
63 ibe a method that uses diethylpyrocarbonate (DEPC) labeling and mass spectrometry to detect three-dim
64 as also assessed using diethylpyrocarbonate (DEPC), which modifies histidines.
65 in were identified via diethylpyrocarbonate (DEPC) labeling and bottom-up proteomics.
66 ical modification with diethylpyrocarbonate (DEPC) and site-directed mutagenesis demonstrating the si
67 sidues of tubulin with diethylpyrocarbonate (DEPC) at a mole ratio of 0.74 (DEPC/total His residues)
68 tems, we show that the slower time scale for DEPC labeling makes it only sensitive to changes in solv
69  substrate myristoyl-ACP protected HlyC from DEPC inhibition.
70 ate was unable to protect heparinase II from DEPC inactivation for either of the substrates.
71                                    In H233D, DEPC targets one less histidine than was measured using
72                                 Importantly, DEPC labeling is able to provide information for up to 3
73  formed from DMPC and for longer channels in DEPC.
74  upon antibody binding generally decrease in DEPC labeling extent.
75 ophobic residues promote a local increase in DEPC concentration such that serine, threonine, and tyro
76 ysis of O,O-diethylphosphorylcholine iodide (DEPC) and the primary (18)O effect in the alkaline hydro
77 ibody binding that presumably increase local DEPC concentrations.
78  in less than 3 min, and as low as 10 microM DEPC results in a 85% loss of heparinase I activity in 1
79 difying diethyl pyrocarbonate (DEPC); 0.3 mM DEPC results in 95% of heparinase I inactivation in less
80                                    Moreover, DEPC inactivates cytochrome b(561) more rapidly at alkal
81 otein structure and function, the ability of DEPC labeling/MS to distinguish histidine tautomers shou
82 ion with heparin followed by the addition of DEPC resulted in a loss of enzymatic activity toward hep
83 ly straightforward mass spectral analysis of DEPC-labeled proteins, we expect this method should be a
84        This result expands the capability of DEPC as a structural probe because about 25% of the sequ
85 occurs due to higher local concentrations of DEPC.
86                               The extents of DEPC modification of the histidine and tyrosine residues
87 lity and histidine reactivity information of DEPC-modified OMD necessary for the design of experiment
88       The inherent problem of instability of DEPC-modified histidine residues was overcome by adjusti
89 k demonstrated the considerable potential of DEPC covalent labeling data to be used for accurate high
90  of the differences in the reaction rates of DEPC and HDX.
91 sary information to describe the reaction of DEPC with OMD.
92  Ferri/ferrocyanide can mediate reduction of DEPC-treated cytochrome b(561) by ascorbic acid, indicat
93 rans DOPC (dielaidoyl phosphatidylcholine or DEPC) on the morphology of giant unilamellar vesicles (G
94                                  Because our DEPC labeling/MS approach is simpler, faster, and more p
95                                     Overall, DEPC labeling of antigen-antibody complexes is found to
96                                     Overall, DEPC-based covalent labeling mass spectrometry offers an
97 holine/1, 2-dielaidoyl-phosphatidylglycerol (DEPC/DEPG) liposomes at pH 5.0 as a function of peptide
98 d 1,2-dierucoyl-sn-glycero-3-phosphocholine (DEPC).
99  diameter was measured by using the proposed DEPC method and compared with flowmeter measurements and
100                                 The proposed DEPC method was sensitive to two velocity regimes within
101 er low specificity of diethyl pyrocarbonate (DEPC) for histidine modification, we modified Tris-washe
102 e histidine-modifying diethyl pyrocarbonate (DEPC) inhibited acyltransferase activity, and acyltransf
103        Treatment with diethyl pyrocarbonate (DEPC) inhibits reduction of the cytochrome by ascorbate,
104                       Diethyl pyrocarbonate (DEPC) modification of isoform E nearly abolishes its cyt
105 rcular dichroism, and diethyl pyrocarbonate (DEPC) modification.
106 tein was reacted with diethyl pyrocarbonate (DEPC) over a range of pH values.
107                       Diethyl pyrocarbonate (DEPC), a histidine residue-specific reagent, completely
108 hydrophobic reagents [diethyl pyrocarbonate (DEPC), p-bromophenacyl bromide] as compared to the more
109 he) is inactivated by diethyl pyrocarbonate (DEPC).
110 i)) is inactivated by diethyl pyrocarbonate (DEPC).
111 e histidine-modifying diethyl pyrocarbonate (DEPC); 0.3 mM DEPC results in 95% of heparinase I inacti
112 ase is inactivated by diethyl pyrocarbonate (DEPC); activity can be fully restored by incubation with
113                       Diethyl pyrocarbonate (DEPC; 10 mM) treatment of P2X4-injected oocytes had no e
114 ormone as model systems, we demonstrate that DEPC labeling can identify both specific protein regions
115 ments on model peptides, we demonstrate that DEPC reacts equally with both tautomeric forms to produc
116 ome b(561) by ascorbic acid, indicating that DEPC-inhibited cytochrome b(561) cannot accept electrons
117            Further evidence for this is that DEPC treatment inhibits oxidation of the cytochrome by s
118 tems, we demonstrate for the first time that DEPC can modify Ser and Thr residues in addition to His
119                                          The DEPC modification was pH dependent and reversible by hyd
120                                 Although the DEPC--MMOB species exhibited only minor changes relative
121                      Differences between the DEPC and conventional SEPC MRI methods were assessed by
122                          Then, with both the DEPC MRI sequence and the conventional single-echo phase
123                  Given the simplicity of the DEPC labeling chemistry and the relatively straightforwa
124 ent of wild-type lyase His-233 as one of the DEPC targets.
125 f oxidants and reductants and removal of the DEPC-histidine adduct by sodium hydroxide.
126                      Characterization of the DEPC-modified Rieske protein, which remains redox active
127 8-P synthase activity is not restored to the DEPC-inactivated enzyme following treatment with hydroxy
128 imes were approximately 19% shorter with the DEPC method (TR, 5.7 msec) than with the SEPC method (TR
129 ds showed that decreasing bilayer thickness (DEPC-POPC-DMPC) led to an increase in the helix tilt ang
130         These mutants were also subjected to DEPC modification, and results are consistent with the p
131                                Finally, when DEPC modification of the protein was carried out in the
132         Double-modification experiments with DEPC and Pt-TP demonstrate that both modifiers affect th
133         Similarly, tubulin modification with DEPC for longer times (8 min) resulted in complete inhib
134      Experiments involving modification with DEPC suggest that a histidine is essential and is protec
135  that these residues almost never react with DEPC in free peptides, supporting the hypothesis that a

 
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