160954
对硝基苯磺酸甲酯
99%
别名:
Methyl nosylate, Methyl p-nitrobenzenesulfonate, Methyl p-nitrotosylate
质量水平
方案
99%
表单
solid
mp
89-92 °C (lit.)
溶解性
acetone: soluble 5%, clear, faintly yellow to greenish-yellow
官能团
nitro
sulfonic acid
SMILES字符串
COS(=O)(=O)c1ccc(cc1)[N+]([O-])=O
InChI
1S/C7H7NO5S/c1-13-14(11,12)7-4-2-6(3-5-7)8(9)10/h2-5H,1H3
InChI key
RMNJNEUWTBBZPT-UHFFFAOYSA-N
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一般描述
Reaction between methyl 4-nitrobenzenesulfonate and bromide ions has been studied in mixed single-chain-gemini micellar solutions. Kinetics of SN2 reactions of methyl 4-nitrobenzenesulfonate with ammonia, primary amines, secondary amines, tertiary amines and anionic nucleophiles has been studied.
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
A Lewendon et al.
The Biochemical journal, 290 ( Pt 1), 15-19 (1993-02-15)
A catalytically essential histidine residue (His-195) of chloramphenicol acetyltransferase (CAT) acts as a general base in catalysis, abstracting a proton from the primary hydroxy group of chloramphenicol. The pKa of His-195 has been determined from the pH-dependence of chemical modification.
Cysteine modification of metallothionein.
P E Hunziker
Methods in enzymology, 205, 399-400 (1991-01-01)
J P Marcus et al.
Archives of biochemistry and biophysics, 316(1), 413-420 (1995-01-10)
Incubation of L-threonine dehydrogenase from Escherichia coli with methyl p-nitrobenzenesulfonate results in a time- and concentration-dependent loss of enzymatic activity. As the concentration of the methylating agent is increased, the rate of inactivation reaches a limiting value of 0.01 min-1
O Paquatte et al.
Photochemistry and photobiology, 50(6), 817-825 (1989-12-01)
Vibrio harveyi luciferase, an alpha beta dimer, was effectively inactivated by treatment with the methylation agent methyl p-nitrobenzene sulfonate. However, inactivation of luciferase in the presence of excess amounts of this reagent did not follow pseudo-first-order kinetics. After taking the
S Ishii et al.
Protein science : a publication of the Protein Society, 7(8), 1802-1810 (1999-03-19)
Aromatic L-amino acid decarboxylase (AADC) catalytic mechanism has been proposed to proceed through two consecutive intermediates (i.e., Michaelis complex and the external aldimine). Limited proteolysis of AADC that preferentially digested at the C-terminal side of Arg334 was slightly retarded in
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