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D6388

Sigma-Aldrich

Dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide

≥95%

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About This Item

Empirical Formula (Hill Notation):
C9H12BrNO3S
CAS Number:
28611-73-6
Molecular Weight:
294.17
EC Number:
249-105-5
MDL number:
MFCD00038741
UNSPSC Code:
12352100
PubChem Substance ID:
57654116
NACRES:
NA.22

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

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Gloves

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Heparin binding and protease inhibitor activity of chemically modified antithrombin III.
M N Blackburn et al.
Annals of the New York Academy of Sciences, 370, 700-707 (1981-01-01)
S Park et al.
Biochemistry, 39(38), 11732-11741 (2000-09-20)
The fluorescence intensity difference between rabbit skeletal myosin subfragment 1 (S1) and nucleotide-bound or trapped S1 isolates ATP-sensitive tryptophans (ASTs) emission from the total tryptophan signal. Neutral (acrylamide) quenching of the ASTs is sensitive to the binding or trapping of
M F Scully et al.
Thrombosis and haemostasis, 65(4), 351-354 (1991-04-08)
Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. Upon
M M Werber et al.
Biochemistry, 26(10), 2903-2909 (1987-05-19)
Modification of tryptophanyl residues (Trps) of myosin subfragments 1 (S-1) was performed with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide (DHNBS). Under controlled conditions, pH 6 at 0 degrees C and 10-min reaction with 10-100-fold molar excess, K+(EDTA) activity was reduced down to less than
G B Villanueva
Biochemistry, 20(23), 6519-6525 (1981-11-10)
The conformations of human alpha-thrombin and gamma-thrombin have been compared by circular dichroism, solvent perturbation different spectroscopy, and chemical modification. Circular dichroism studies indicate that proteolytic conversion of alpha-thrombin to gamma-thrombin is accompanied by considerable conformational changes which include a
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