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N7251

Sigma-Aldrich

4-Nitrocatechol sulfate dipotassium salt

crystalline

Sinónimos:

2-Hydroxy-5-nitrophenyl sulfate, 2-Hydroxy-5-nitrophenyl sulfate dipotassium salt monohydrate, p-Nitrocatechol sulfate dipotassium salt

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About This Item

Fórmula lineal:
C6H3NO7SK2
Número de CAS:
14528-64-4
Peso molecular:
311.35
Beilstein/REAXYS Number:
3805018
EC Number:
238-550-0
MDL number:
MFCD00007465
UNSPSC Code:
12352200
PubChem Substance ID:
24897816
NACRES:
NA.77

form

crystalline

Quality Level

100

color

yellow

storage temp.

−20°C

SMILES string

[K+].[K+].[O-]c1ccc(cc1OS([O-])(=O)=O)[N+]([O-])=O

InChI

1S/C6H5NO7S.2K/c8-5-2-1-4(7(9)10)3-6(5)14-15(11,12)13;;/h1-3,8H,(H,11,12,13);;/q;2*+1/p-2

InChI key

CKWWBDCAYRJAJB-UHFFFAOYSA-L

General description

4-Nitrocatechol sulfate is an aromatic sulfate.

Application

4-Nitrocatechol sulfate dipotassium salt has been used as a substrate in mucopolysaccharidoses VI (MPS VI) analysis. It has also been used to measure the activity of glycosaminoglycan (GAG)-degrading enzymes-arylsulfatase B, and exoglycosidases.

Substrates

Chromogenic sulfatase substrate.

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Gloves

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M Lee-Vaupel et al.
Clinica chimica acta; international journal of clinical chemistry, 164(2), 171-180 (1987-04-30)
Arylsulfatase A hydrolyzes the artificial chromogenic substrate 4-nitrocatechol-sulfate at 0 degree C at a rate of 24% of that at 37 degrees C whereas arylsulfatase B is almost inactive at 0 degree C. Based on this observation, a simple assay
M Recksiek et al.
The Journal of biological chemistry, 273(11), 6096-6103 (1998-04-16)
Sulfatases contain an active site formylglycine residue that is generated by post-translational modification. Crystal structures of two lysosomal sulfatases revealed significant similarity to the catalytic site of alkaline phosphatase containing a serine at the position of formylglycine. To elucidate the
Mazdak Khajehpour et al.
Biochemistry, 46(14), 4370-4378 (2007-03-14)
The Yersinia protein tyrosine phosphatase (YopH) contains a loop of ten amino acids (the WPD loop) that covers the entrance of the active site of the enzyme during substrate binding. In this work the substrate mimicking competitive inhibitor p-nitrocatechol sulfate
C O'Fagain et al.
The Biochemical journal, 201(2), 345-352 (1982-02-01)
A simple model is described to account for the anomalous time course of arylsulphatase A. In the case of the ox liver and human placental enzymes the enzyme-nitrocatechol sulphate complex can, in addition to forming products, slowly break down to
S Partanen
The Histochemical journal, 16(5), 501-506 (1984-05-01)
A new, direct-colouring, metal precipitation method for the light microscopical demonstration of arylsulphatases A and B is described. It is based on the reducing capacity of nitrocatechol liberated by arylsulphatases from p-nitrocatechol sulphate. The reaction is carried out in Karnovsky-Roots'
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Protocolos

Enzymatic Assay of Sulfatase (EC 3.1.6.1.)

Enzymatic Assay of Sulfatase (EC 3.1.6.1.)

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