ライフサイエンスコーパス: DTNB

1 DTNB alone and in combination with mibefradil induces th

2 DTNB reduction was inhibited by 0.2 mM arsenite.

3 DTNB reversed these kinetic effects.

4 DTNB, glutathione disulfide, and cystine were only margi

5 DTNB-modified APX (APX-TNB) exhibits only 1.3% wild-type

6 DTNB-treated TPH [sulfhydryl (SH)-protected] exposed to

7 model consistent with these data involves a DTNB-induced mixed disulfide linkage between C93 and C10

8 The assay uses dithiobisnitrobenzoic acid (DTNB) to detect coenzyme A (CoASH) release on acetylatio

9 imide (NEM) and bis-dithionitrobenzoic acid (DTNB) prevented covalent activation; the effect of DTNB

10 o inhibited by 5,5'-dithionitrobenzoic acid (DTNB).

11 H3 with 5,5'-dithio-bis(2-nitrobenzoic acid (DTNB) and to directly add the histones to DNA at physiol

12 ol-active reagent, dithio-nitrobenzoic acid (DTNB), is used to probe the exposure of the cysteine sid

13 en, and 5,5'-dithio-bis-2-nitrobenzoic acid (DTNB).

14 agent 5,5'-dithio-bis(2-nitrobenzoic) acid (DTNB) had any effect on 3H-aspartate transport suggestin

15 s using 5,5'-dithiobis-(2nitrobenzoic acid) (DTNB) (Ellman's reagent) that show protein disulfides to

16 MTS) or 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) also compromised the Zn(2+) binding properties of

17 Based on 5,5-dithiobis(2-nitrobenzoic acid) (DTNB) and AhpC reactivity with multiple mutants of AhpF,

18 trons to 5,5'-dthiobis(2-nitrobenzoic acid) (DTNB) and AhpC.

19 idant 5, 5'-dithio-bis(2-nitrobenzoic acid) (DTNB) and the redox cofactor pyrroloquinoline quinone (P

20 agent 5,5'-dithio-bis-(2-nitrobenzoic acid) (DTNB) and the T channel antagonist mibefradil.

21 gent 5, 5'-dithio-bis-(2-nitrobenzoic acid) (DTNB) caused inhibition.

22 lfide 5,5'-dithio-bis (2-nitrobenzoic acid) (DTNB) causes an inactivation of TPH that is readily reve

23 MPS and 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) cysteine reactivities indicated that the cysteines

24 dues to 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) indicated that wild-type RPA contained 8.2 reactiv

25 eagent 5,5'-dithiobis (2-nitrobenzoic acid) (DTNB) is used.

26 vities [5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) reductase, oxidase, transhydrogenase, and, in the

27 late or 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) resulted in the generation of derivatives whose bi

28 gs of 5-5'-Dithio-bis (2-nitrobenzoic acid) (DTNB) solutions were examined.

29 eagent 5,5'-dithio-bis(2-nitrobenzoic acid) (DTNB) to form the yellow derivative 5'-thio-2-nitrobenzo

30 tion of 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) were overcome.

31 eagent 5,5'-dithio-bis(2-nitrobenzoic acid) (DTNB) with the type-I MetAP from E. coli and the type-II

32 tion of 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB), and reduction of insulin in the presence of thior

33 sulin, 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB), and the manganese-containing type Ib ribonucleoti

34 tivity--5'5-dithio-bis(2-nitrobenzoic acid) (DTNB), bacitracin, and anti-protein disulfide isomerase

35 NEM) or 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB), indicating IRP2 contains a cysteine(s) that is (a

36 uous, 5,5'-dithio-bis-(2-nitrobenzoic acid) (DTNB)-based assay for the CBS-catalyzed hydrolysis of L-

37 5,5'-Dithiobis(2-nitrobenzoic acid) (DTNB, or Ellman's reagent) was used for the oxidation.

38 dant (5, 5'-dithio-bis[2-nitrobenzoic acid], DTNB), or the noncompetitive antagonist CP101,606 (CP).

39 ium after low Mg(2+)-induced ictal activity, DTNB significantly inhibited NMDAR-mediated currents, in

40 large in the absence of denaturant to allow DTNB unhindered access.

41 A kinetic model of the effects of DTT and DTNB suggested that the receptor existed in equilibrium

42 , resulted in reduced sensitivity to DTT and DTNB.

43 were considerably less sensitive to DTT and DTNB.

44 eading to complete loss of hydroperoxide and DTNB reductase activities.

45 The pH dependence of methylation and DTNB modification reactions, and spectroscopic propertie

46 These data suggested that PQQ and DTNB suppressed spontaneous ictal activity by reversing

47 All MerB cysteines are DTNB-reactive in native and denatured states except Cys1

48 strates (i) with good leaving groups such as DTNB, (ii) that are highly electrophilic such as selenit

49 in slices exposed to 4-7 microM bicuculline, DTNB and PQQ reversed the potentiation of evoked epilept

50 Both DTNB and AhpC reduction by AhpF are dramatically affecte

51 ppears that the ascorbate site is blocked by DTNB modification which is well removed from the exposed

52 to quantify Zn(II) and reduced cysteine (by DTNB reactivity) content, reveal Zn(II)/MTF-zf stoichiom

53 n on SDS PAGE and a loss of two cysteines by DTNB titrations, consistent with disulfide formation.

54 reased by TCEP and subsequently decreased by DTNB or PQQ at the same concentrations that modulated ep

55 nts were potentiated by DTT and inhibited by DTNB.

56 activity was determined to be 31 units/mg by DTNB assay.

57 glone, ninhydrin, alloxan, dehydroascorbate, DTNB, lipoic acid/lipoamide, S-nitrosoglutathione, selen

58 NADH-dependent DTNB reduction, on the other hand, requires communicatio

59 catalytic activities in the NADPH-dependent DTNB [5,5'-dithiobis(2-nitrobenzoate)] assay.

60 hese mutations, dropping to less than 5% for DTNB reductase activity and to less than 2% for peroxida

61 n 25 and 8 times greater can be achieved for DTNB detection using AuNPs@mesoSiO2 compared with the no

62 Apparent Km values for DTNB, Escherichia coli Trx, and rat Trx were 116, 34, an

63 The enzyme was protected from DTNB-induced inactivation by inclusion of the substrate

64 or in the presence of oxidized glutathione, DTNB-reactive thiols of the plasma membrane are decrease

65 However, DTNB and PQQ had little effect on baseline NMDA-evoked c

66 ld increase in sensitivity over the improved DTNB titration method.

67 The inhibitors DTNB and bacitracin blocked the detection of these free

68 Likewise, L-cysteine induces mechanical DTNB-sensitive hyperalgesia in peripheral receptive fiel

69 lesser extent, dithio(bis)-p-nitrobenzoate (DTNB), improved the heat stability of WPI; these reagent

70 ng reagents 5,5-dithiobis (2-nitrobenzoate) (DTNB) and methyl methanethiosulfonate (MMTS).

71 groups with 5,5'-dithiobis(2-nitrobenzoate) (DTNB) under carefully controlled conditions has extended

72 (MMTS) and 5,5'-dithiobis(2-nitrobenzoate) (DTNB), including the appropriate Cys --> Ser mutants, de

73 contained 11 5,5-dithiobis(2-nitrobenzoate) (DTNB)-titratable sulfhydryl (SH) groups.

74 Addition of DTNB to cells followed by disulfide addition directly me

75 prevented covalent activation; the effect of DTNB was reversed by reduction with DTT.

76 n into folding conditions in the presence of DTNB allowed the degree of sidechain protection in any r

77 d by mass spectrometry (MS) from reaction of DTNB with the C59A and C70A mutant EcMetAP-I enzymes.

78 Reactions of DTNB with the C109A/C116A double mutant showed that C93

79 to disulfide-containing substrates (AhpC or DTNB), and ultimately to peroxides from AhpC.

80 reactions--(i) the thiol-alkylating reagent DTNB (5,5'-dithiobis[2-nitrobenzoic acid]), (ii) bacitra

81 adily accessible to the modification reagent DTNB and therefore inactivation may result from structur

82 are inaccessible to the modification reagent DTNB, indicating that they are located in the interior o

83 le Cys residue in APX with Ellman's reagent (DTNB) blocks the ability of APX to oxidize ascorbate but

84 ereas thioredoxin 2 (Trx2) could only reduce DTNB.

85 between red wines sulfite value by standard DTNB (5,5'-dithio-bis-(2-nitrobenzoic acid)) method and

86 Verification that DTNB covalently binds to C59 in EcMetAP-I was obtained b

87 correlation between the SERS signal and the DTNB concentration was found to be linear within a range

88 cence assay, glutathione (GSH) levels by the DTNB-GSSG reductase method, apoptosis, reactive oxygen s

89 on may result from structural changes in the DTNB-modified KDO 8-P synthase or blockage of access of

90 Cyanolysis of the DTNB-inactivated enzyme with KCN led to the elimination

91 Isolation and chemical analysis of the DTNB-treated GIF derivative revealed that binding the 5-

92 nal scale spectrophotometric assays with the DTNB method (412 nm) for CoASH production or by monitori

93 Zinc-finger cysteines slowly reacted to DTNB as compared to others.

94 y (a) reactivity of cysteine residues toward DTNB [5, 5'-dithiobis(2-nitrobenzoic acid)] and a thiol-

95 f enzymatic activity and the presence of two DTNB-titratable cysteine residues.

96 ower than that for NADPH when analyzed using DTNB reductase assays).

97 Titration of native C38A and C166A with DTNB resulted in modification of two cysteines while tit

98 quency of channel opening when compared with DTNB.

99 Titration of denatured enzyme with DTNB resulted in the modification of all four cysteines.

100 Titration of the next 3.0 SH groups with DTNB resulted in a loss of activity of more than 70%.

101 n and measured the kinetics of labeling with DTNB over a range of urea concentrations.

102 titrations, and the reaction of DGD-PLP with DTNB is tentatively assigned to the conformational chang

103 OR pretreated with DTNB was protected from inhibition by phenoxyl radicals

104 e mutant arrestin R175Q reacted rapidly with DTNB, but not as rapidly as with SDS-denatured arrestin.

105 tes except Cys117, which fails to react with DTNB in the native form, suggesting it is buried.

106 hree cysteines in bovine arrestin react with DTNB very slowly (over a period of several hours).

107 nthase, and both native mutants reacted with DTNB to modify only one of the three remaining cysteine

108 ive enzyme 1.0 SH group readily reacted with DTNB with no detectable loss of activity.

109 Studies of reactions with DTNB show that both cysteines are reactive and exhibit b

110 ctivity, Zn(2+) content, and reactivity with DTNB.

111 ed near residue Cys(2113), which reacts with DTNB, and (4) binding to a PS-containing membrane is an

112 ction of cloned native KDO 8-P synthase with DTNB correlated with modification of two of the four cys

113 g media and measuring the reduced thiol with DTNB (Ellman's reagent).

114 th MMTS, no cysteines could be titrated with DTNB and no enzymatic activity could be detected.