D6388
Dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide
≥95%
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About This Item
Recommended Products
Assay
≥95%
form
solid
storage temp.
2-8°C
SMILES string
[Br-].C[S+](C)Cc1cc(ccc1O)[N+]([O-])=O
InChI
1S/C9H11NO3S.BrH/c1-14(2)6-7-5-8(10(12)13)3-4-9(7)11;/h3-5H,6H2,1-2H3;1H
InChI key
VEGVMTIJKACZGO-UHFFFAOYSA-N
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Structure-function relationship in the allosteric L-lactate dehydrogenases from Lactobacillus casei and Lactobacillus curvatus.
European journal of biochemistry, 126(3), 549-558 (1982-09-01)
FEBS letters, 259(2), 346-348 (1990-01-01)
Rabbit skeletal muscle myosin subfragment-1 (S-1) was reacted with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide (DHNBS) resulting in modification of 0.8 tryptophan residues per S-1. In order to assign the most reactive tryptophan of the 5 S-1 tryptophans, antibodies were raised in rabbits against
Biochemistry, 40(7), 2194-2200 (2001-05-01)
Brequinar and the active metabolite of leflunomide, A77 1726, have been clearly shown to inhibit human dihydroorotate dehydrogenase (DHODH), but conflicting mechanisms for their inhibition have been reported. DHODH catalyses the conversion of dihydroorotate (DHO) to orotate concurrent with the
Inactivation of the nucleoside transporter of the human erythrocyte by dimethyl (2-hydroxy-5-nitrobenzyl) sulphonium bromide.
Biochemical Society transactions, 19(4), 418S-418S (1991-11-01)
Archives of biochemistry and biophysics, 233(2), 712-720 (1984-09-01)
A single tryptophan residue on antithrombin has been modified with dimethyl-(2-hydroxy-5-nitrobenzyl)sulfonium bromide. This alteration led to a 500-fold reduction in the heparin-dependent acceleration of thrombin-modified antithrombin interactions, as well as a 10-fold decrease in the avidity of the modified protease
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