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1 ng thiol like DTT (dithiothreitol) and 2-ME (2-mercaptoethanol).
2 strongly inhibited by high concentrations of 2-mercaptoethanol.
3 is significantly quenched by 450-fold excess 2-mercaptoethanol.
4 activate GABA-AT, but only in the absence of 2-mercaptoethanol.
5 dependent inhibitor, even in the presence of 2-mercaptoethanol.
6 th o-phthalaldehyde (OPA) in the presence of 2-mercaptoethanol.
7 ation by H2O2 or reduction by glutathione or 2-mercaptoethanol.
8  mercuric chloride was readily reversible by 2-mercaptoethanol.
9 nd destabilized by D-ribulose-5-phosphate or 2-mercaptoethanol.
10  be completely suppressed by the addition of 2-mercaptoethanol.
11 vity of FDH occurred only in the presence of 2-mercaptoethanol.
12 s is subsequently achieved with an excess of 2-mercaptoethanol.
13 ted to the 31-kDa band by the reducing agent 2-mercaptoethanol.
14 e GR active site with thiol reagents such as 2-mercaptoethanol.
15  (300 microM) and the lipophilic antioxidant 2-mercaptoethanol (10 microM) both protected significant
16 100 (20 mm), PA (2 mm), Mg(2+) (0.5 mm), and 2-mercaptoethanol (10 mm) at pH 7.5 and 30 degrees C.
17 nd L(R, S) recovered fully after transfer to 2-mercaptoethanol (10 mM).
18                 Treatment of these sera with 2-mercaptoethanol (2-ME) reduced, but did not eliminate,
19 than structurally similar monothiols such as 2-mercaptoethanol (2-ME), that cleavage by DTT exhibits
20 elation coefficient between IgG anti-LPS and 2-mercaptoethanol (2-ME)-resistant vibriocidal antibodie
21 .0 unit/mL) with heat (95 degrees C, 5 min), 2-mercaptoethanol (2-ME, 0.83 %), and l-cysteine (l-Cys,
22 by epidermal growth factor, we found that 2-(2-mercaptoethanol)-3-methyl-1,4-naphthoquinone or Compou
23           A synthetic vitamin K analogue, 2-(2-mercaptoethanol)-3-methyl-1,4-naphthoquinone or compou
24  shown that a synthetic vitamin K analog, 2-(2-mercaptoethanol)-3-methyl-1,4-naphthoquinone or compou
25                     Compound 5 (Cpd 5) or 2-(2-mercaptoethanol)-3-methyl-1,4-naphthoquinone, is an in
26  probed the effects of a Cdc25 inhibitor, 2-(2-mercaptoethanol)-3-methyl-1,4-naphthoquinone, or Compo
27            Treatment of protein samples with 2-mercaptoethanol abolished the S-thiolation signals det
28 n of the NCS-chrom C-6 radical, generated by 2-mercaptoethanol activation, to C-5 of the uracil at th
29  presumably due to their purification (i.e., 2-mercaptoethanol adducts and carbamylation) and related
30 ts such as tris(2-carboxyethyl)phosphine and 2-mercaptoethanol also abrogate NS5A-NS5A interactions,
31 y-7,8-dihydrobenzo[a]pyrene was trapped with 2-mercaptoethanol and characterized as a thioether conju
32 activity was demonstrated in the presence of 2-mercaptoethanol and dithiothreitol.
33                                  Two thiols, 2-mercaptoethanol and mercapto-2-propanol, were poorer s
34 K activation was blocked by the antioxidants 2-mercaptoethanol and N-acetyl-L-cysteine, suggesting th
35 M Tris (pH 7.5), 6 mM NaCl, 5 mM MgCl2, 5 mM 2-mercaptoethanol, and 10% (v/v) glycerol, 4 degrees C].
36 ris-HCl, pH 7.5, 6 mM NaCl, 5 mM MgCl2, 5 mM 2-mercaptoethanol, and 10% (v/v) glycerol, 4.0 degrees C
37  was observed with cysteine, dithiothreitol, 2-mercaptoethanol, and 3-mercaptopropionate.
38      The CoM analogues 2-mercaptopropionate, 2-mercaptoethanol, and cysteine substituted poorly for C
39 activation of spinach PRK by dithiothreitol, 2-mercaptoethanol, and glutathione was examined.
40 ut not with sodium dodecyl sulfate (SDS) and 2-mercaptoethanol, and migrated as polydisperse, high-mo
41                Reducing agents, such as DTT, 2-mercaptoethanol, and thioredoxin, were able to activat
42 tivity toward thiols like dithiothreitol and 2-mercaptoethanol as well as reagents: mixed disulfides
43                                              2-Mercaptoethanol assists in the conversion of monomers
44                   The free radical scavenger 2-mercaptoethanol completely suppressed ROS generation b
45  Proteins extracted from coats with urea and 2-mercaptoethanol could, after removal of urea by gel fi
46 hy/mass spectrometry of the o-phthalaldehyde/2-mercaptoethanol derivatives and identified as citrulli
47                                              2-Mercaptoethanol, glutathione, dithiothreitol, and thio
48 n the presence of Co(2+), Mn(2+)or Mg(2+)and 2-mercaptoethanol in cacodylate or HEPES buffer, pH 7.2,
49                                 Inclusion of 2-mercaptoethanol in the upper electrode buffer greatly
50  show that the use of a shorter diluent like 2-mercaptoethanol is more advantageous than using a long
51                    To assess the efficacy of 2-mercaptoethanol/L-cysteine mixed disulfide (CySSME) as
52 r employing sodium dodecyl sulfate (SDS) and 2-mercaptoethanol (ME) resulted in 39.5% and 29.5%, resp
53 T), 2-(diethylamino)ethanethiol (DEAET), and 2-mercaptoethanol (ME) with o-phthaldialdehyde in the pr
54 essfully as co-substrates were thiosulphate, 2-mercaptoethanol, mercaptoacetate and aminoethylthiopse
55                   Heating and reduction with 2-mercaptoethanol of GIF resulted in the release of a ap
56 harsh conditions such as treatment with pure 2-mercaptoethanol or treatment with boiling water for 5
57                 Pretreatment of corneas with 2-mercaptoethanol prevented the effects of Hg2+ on the p
58 wo other antioxidants, N-acetyl cysteine and 2-mercaptoethanol, reduced growth and viability of MO7e
59                           The reducing agent 2-mercaptoethanol significantly attenuates filament asse
60 th compound 8a and subsequent treatment with 2-mercaptoethanol/sodium methoxide afforded the guanine
61                          Upon reduction with 2-mercaptoethanol the mass of this product decreased to
62 some cysteine residues were derivatized with 2-mercaptoethanol to form S,S-(2-hydroxyethyl)thiocystei
63 tions of amino acids with o-phthaldialdehyde/2-mercaptoethanol to generate electroactive derivatives
64                                              2-Mercaptoethanol was a weak competitive inhibitor vs Co
65                         A preincubation with 2-mercaptoethanol was also included for optimal permeabi
66 protein from B. subtilis cells when urea and 2-mercaptoethanol were used in breakage buffers, implyin
67 ch as acetate, and by thiols such as GSH and 2-mercaptoethanol, which disrupt its stabilizing double
68 n and FDH was independent of the presence of 2-mercaptoethanol while 10-FDDF dehydrogenase activity o
69  in PBS but became fluorescent after SDS and 2-mercaptoethanol, with a quenching capacity of 10-fold