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1 action with strong reducing reagents such as sodium dithionite).
2 ectron-reduced species during titration with sodium dithionite.
3 ted by treating cells with sodium sulfite or sodium dithionite.
4 of outer leaflet probe with externally added sodium dithionite.
5 nd then exposed to the hemoprotein reductant sodium dithionite (1 mmol/L) under N(2), there is a part
6 nverted to the reduced form upon addition of sodium dithionite and hydrogen.
7 reductive titrations of CODH/ACS with CO and sodium dithionite and monitored the reaction by electron
8                 Reduction of the mutant with sodium dithionite and reoxidation with Me(2)SO, however,
9     The diferric cluster could be reduced by sodium dithionite, and the diferrous state was found to
10 nes were next reduced to aminotyrosines with sodium dithionite, and-at pH 5.0-cleavable biotin tags w
11 d pterin-free iNOS(heme) was examined, using sodium dithionite as the reductant.
12 n assays containing SAM, BChlide c or d, and sodium dithionite, BciD catalyzed the conversion of SAM
13 d-type PS I, reduction of F(A) and F(B) with sodium dithionite causes a approximately 30% increase in
14 m to the wild-type protein and is reduced by sodium dithionite, demonstrating that it is a flavin-bin
15                                   Additional sodium dithionite first produces some neutral, blue flav
16 NT is reduced to 3-aminotyrosine (3AT) using sodium dithionite followed by derivatization of light an
17 bated with GTP, S-adenosyl-L-methionine, and sodium dithionite in the absence of MoaC.
18                         After reduction with sodium dithionite in the presence of light, approximatel
19 here that when a HbRC core is incubated with sodium dithionite in the presence of light, the 15 ms ch
20                     Reductive titration with sodium dithionite indicates heme reduction takes place p
21                     In contrast, proline and sodium dithionite induce tight binding of PutA to the li
22                                              Sodium dithionite is added subsequently to reduce the ni
23 din to emodin hydroquinone, for example with sodium dithionite, is obligatory for the enzymatic reduc
24 obic reduction of the ferric-NO species with sodium dithionite led to the formation of two spectrally
25                                              Sodium dithionite (Na(2)S(2)O(4)), lowering pO(2) to 10
26 ncreased when [Ca2+]o was doubled.Hypoxia by sodium dithionite (Na2S2O4) induced large [Ca2+]i increa
27  Reduction of the Hox sample with 100% H2 or sodium dithionite (NaDT) nearly eliminated the 2.1 signa
28                        Reduction with either sodium dithionite or dithiothreitol decreased the copper
29                           In the presence of sodium dithionite or in the presence of P. aeruginosa fe
30 itrations show that approximately 1 equiv of sodium dithionite or NADPH is required to fully reduce C
31       Anaerobic reduction of the enzyme with sodium dithionite or substrate yields no detectable semi
32 ls and treating them with the reducing agent sodium dithionite prior to EPR measurements.
33  Reduction of this RRE reaction product with sodium dithionite produces the one-electron-reduced RRE,
34                                         When sodium dithionite-reduced LipA was incubated with octano
35                                  Under H2 or sodium dithionite reductive treatments, the EPR spectra
36             Titration of the FMN domain with sodium dithionite resulted in the conversion of the prot
37                       Reduction of emodin by sodium dithionite resulted in the formation of two tauto
38 ctants, and anaerobic reduction of BioB with sodium dithionite results in conversion to enzyme contai
39                               Reduction with sodium dithionite results in small quantities of an S =
40 tion of the TMADH x ETF protein complex with sodium dithionite shows that a total of five electrons a
41 er, we confirm that it is the reducing agent sodium dithionite that facilitates release of CO from th
42           When BMR is titrated with NADPH or sodium dithionite under anaerobic conditions, addition o
43 n greatly increases the rate of reduction by sodium dithionite when compared to pentacoordinate hemog
44 e of CO in protein solutions alone i.e. when sodium dithionite, widely used in previous studies of CO

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