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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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
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
V.L. Boyd et al.
Tetrahedron Letters, 31, 3849-3849 (1990)
S R Rao et al.
Indian journal of biochemistry & biophysics, 34(3), 253-258 (1997-06-01)
Maize leaf NADP-malic enzyme was rapidly inactivated by micromolar concentrations of Woodward's reagent K (WRK). The inactivation followed pseudo-first order reaction kinetics. The order of reaction with respect to WRK was 1, suggesting that inactivation was a consequence of the
C T Chang et al.
Biochemistry and molecular biology international, 45(2), 371-380 (1998-07-25)
beta-N-Acetylhexosaminidase was purified from the extract of cabbage by sequential steps of ammonium sulfate fractionation, chromatofocusing, DEAE-Sepharose CL-6B ion exchange chromatography and Sephacryl S-200 HR gel filtration. By these steps, the purity of the enzyme increased by 256 fold with
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