D6388
二甲基(2-羟基-5-硝基苄基)溴化锍
≥95%
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关于此项目
经验公式（希尔记法）:
C9H12BrNO3S
化学文摘社编号:
分子量:
294.17
NACRES:
NA.22
PubChem Substance ID:
UNSPSC Code:
12352100
EC Number:
249-105-5
MDL number:
Assay:
≥95%
Form:
solid
InChI key
VEGVMTIJKACZGO-UHFFFAOYSA-N
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
SMILES string
[Br-].C[S+](C)Cc1cc(ccc1O)[N+]([O-])=O
assay
≥95%
form
solid
storage temp.
2-8°C
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
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)
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
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
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
C B Peterson et al.
The Journal of biological chemistry, 262(16), 7552-7558 (1987-06-05)
Heparin has been shown to exhibit lower affinity for the antithrombin-thrombin complex than for antithrombin alone (Carlstrom, A.-S., Lieden, K., and Bjork, I. (1977) Thromb. Res. 11, 785-797), suggesting that structural alterations in antithrombin may accompany its reaction with thrombin.
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