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About This Item
经验公式（希尔记法）:
C8H11ClO2
CAS号:
分子量:
174.62
Beilstein:
2326749
MDL编号:
UNSPSC代码:
41116107
PubChem化学物质编号:
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技术
HPLC: suitable
gas chromatography (GC): suitable
mp
161-164 °C (lit.)
包装形式
neat
储存温度
−20°C
SMILES字符串
CC1(C)CC(=O)C(Cl)C(=O)C1
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应用
Refer to the product′s Certificate of Analysis for more information on a suitable instrument technique. Contact Technical Service for further support.
底物
Substrate for chloroperoxidase.
储存分类代码
13 - Non Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
A J Kettle et al.
The Biochemical journal, 252(2), 529-536 (1988-06-01)
Myeloperoxidase catalyses the conversion of H2O2 and Cl- to hypochlorous acid (HOCl). It also reacts with O2- to form the oxy adduct (compound III). To determine how O2- affects the formation of HOCl, chlorination of monochlorodimedon by myeloperoxidase was investigated
R D Libby et al.
The Journal of biological chemistry, 265(25), 14808-14811 (1990-09-05)
The kinetics of chloroperoxidase-catalyzed bromination and chlorination reactions were studied at various halide and hydrogen peroxide concentrations. At very high concentrations, both chloride (KI = 370 mM) and bromide (KI = 150 mM) are competitive substrate inhibitors versus hydrogen peroxide.
A J Kettle et al.
The Biochemical journal, 263(3), 823-828 (1989-11-01)
Stimulated neutrophils discharge large quantities of superoxide (O2.-), which dismutates to form H2O2. In combination with Cl-, H2O2 is converted into the potent oxidant hypochlorous acid (HOCl) by the haem enzyme myeloperoxidase. We have used an H2O2 electrode to monitor
P Barnett et al.
The Journal of biological chemistry, 273(36), 23381-23387 (1998-08-29)
Here we describe the isolation, purification, and basic kinetic parameters of a vanadium type chloroperoxidase from the hyphomycete fungus Embellisia didymospora. The enzyme proved to possess similar high substrate affinities, a Km of 5 microM for a bromide, 1.2 mM
Tina Kirchner et al.
Archives of biochemistry and biophysics, 495(1), 21-27 (2009-12-19)
The heme-containing enzyme myeloperoxidase (MPO) accumulates at inflammatory sites and is able to catalyse one- and two-electron oxidation reactions. Here it is shown that (-)-epicatechin, which is known to have numerous beneficial health effects, in low micromolar concentration enhances the
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