95440
2-Ethyl-5-phenylisoxazolium-3′-sulfonate
purum, ≥97.0% (T)
Synonym(s):
Woodwards reagent K
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About This Item
Empirical Formula (Hill Notation):
C11H11NO4S
CAS Number:
Molecular Weight:
253.27
Beilstein:
4149224
EC Number:
MDL number:
UNSPSC Code:
12352005
PubChem Substance ID:
Recommended Products
grade
purum
Assay
≥97.0% (T)
mp
216-219 °C (dec.)
SMILES string
CC[n+]1ccc(o1)-c2cccc(c2)S([O-])(=O)=O
InChI
1S/C11H11NO4S/c1-2-12-7-6-11(16-12)9-4-3-5-10(8-9)17(13,14)15/h3-8H,2H2,1H3
InChI key
MWOOKDULMBMMPN-UHFFFAOYSA-N
Other Notes
Modification of carboxylic groups in enzymes; Coupling reagent for peptide synthesis
replaced by
Product No.
Description
Pricing
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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A A Komissarov et al.
The Journal of biological chemistry, 270(17), 10050-10055 (1995-04-28)
Woodward's reagent K (WRK) completely inactivated Escherichia coli uridine phosphorylase by reversible binding in the active site (Ki = 0.07 mM) with subsequent modification of a carboxyl (k2 = 1.2 min-1). Neither substrate alone protected uridine phosphorylase from inactivation. The
M S Saini et al.
Biochimica et biophysica acta, 568(2), 370-376 (1979-06-06)
Treatment of homogenous human prostatic acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2) with low concentrations of Woodward's reagent K (N-ethyl-5-phenylisoxazolium-3'-sulfonate) leads to a rapid loss of enzymic activity. The rate of inactivation of the enzyme is reduced in the
Hassan Faridnouri et al.
Bioelectrochemistry (Amsterdam, Netherlands), 82(1), 1-9 (2011-07-01)
This work describes the reaction mechanism for chemical modification of tyrosinase by Woodward's Reagent K and its covalent attachment to a glassy carbon electrode. The spectrophotometric studies revealed that the modification does not cause a significant structural change to tyrosinase.
P Paoli et al.
The Biochemical journal, 328 ( Pt 3), 855-861 (1998-02-07)
The organ common-type (CT) isoenzyme of acylphosphatase is inactivated by Woodward's reagent K (WRK) (N-ethyl-5-phenylisoxazolium-3'-sulphonate) at pH6.0. The inactivation reaction follows apparent pseudo first-order kinetics. The dependence of the reciprocal of the pseudo first-order kinetic constant (kobs) on the reciprocal
W Feng et al.
Molecular membrane biology, 13(2), 85-93 (1996-04-01)
In this work we show that ryanodine binding to junctional sarcoplasmic reticulum (SR) membranes or purified ryanodine receptor (RyR) is inhibited in a time- and concentration-dependent fashion by prior treatment with the carboxyl reagent dicyclohexylcarbodiimide (DCCD). Exposure of the membrane-bound
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