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Key Documents

N1252

Sigma-Aldrich

4-Nitrophenyl β-D-galacto­pyran­oside

≥98% (enzymatic),≥98% (TLC), powder

Synonyme(s) :

p-Nitrophenyl β-D-galacto­pyran­oside

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About This Item

Formule empirique (notation de Hill):
C12H15NO8
Numéro CAS:
Poids moléculaire :
301.25
Numéro Beilstein :
92213
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
ID de substance PubChem :
Nomenclature NACRES :
NA.32

product name

4-Nitrophenyl β-D-galacto­pyran­oside, ≥98% (enzymatic)

Pureté

≥98% (TLC)
≥98% (enzymatic)

Forme

powder

Solubilité

water: 10 mg/mL, clear, colorless to very faintly green

Température de stockage

−20°C

Chaîne SMILES 

OC[C@H]1O[C@@H](Oc2ccc(cc2)[N+]([O-])=O)[C@H](O)[C@@H](O)[C@H]1O

InChI

1S/C12H15NO8/c14-5-8-9(15)10(16)11(17)12(21-8)20-7-3-1-6(2-4-7)13(18)19/h1-4,8-12,14-17H,5H2/t8-,9+,10+,11-,12-/m1/s1

Clé InChI

IFBHRQDFSNCLOZ-YBXAARCKSA-N

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Application

4-Nitrophenyl β-D-galactopyranoside has been used:
  • as a substrate to assess the activity of glycosaminoglycan (GAG)-degrading enzymes
  • as a substrate to study the kinetic properties of recombinant Leuconostoc mesenteroides glycosidase (BgLm1) and determine β-glucosidase activity
  • to prepare substrate solution in a modified universal buffer

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Identification, purification and characterization of a novel glycosidase (BgLm1) from Leuconostoc mesenteroides
del Pino-Garcia R, et al.
LWT--Food Science and Technology null
Irina Smirnova et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(37), 15147-15151 (2011-09-08)
The lactose permease (LacY) catalyzes galactoside/H(+) symport via an alternating access mechanism in which sugar- and H(+)-binding sites in the middle of the molecule are alternatively exposed to either side of the membrane by opening and closing of inward- and
Seçil Onal et al.
Artificial cells, blood substitutes, and immobilization biotechnology, 31(3), 339-355 (2003-08-09)
alpha-Galactosidase (alpha-D-galactoside galactohydrolase, EC 3.2.1.22) from watermelon was covalently immobilized on chitin. The immobilized alpha-galactosidase exhibited an activity of 0.61 U per g of carrier and an activity yield of 67%. The properties of free and immobilized alpha-galactosidase were also
Hala Nehme et al.
Analytica chimica acta, 722, 127-135 (2012-03-27)
Enzymes are often quantified by measuring their biological activity. Capillary electrophoresis is gaining its position in this field due to the ongoing trend to miniaturize biochemical assays. The aim of this work was to compare pre-capillary (off-line) and in-capillary electrophoresis
Xuesen Hu et al.
Archiv der Pharmazie, 344(2), 71-77 (2011-02-04)
This experiment was designed to synthesize 18 kinds of polyhydroxybenzophenones by using Friedel-Crafts reaction, and to measure the inhibitory activity on α-glucosidase with p-nitrophenyl-β-D-galactopyranoside (PNPG) as a substrate. Here, acarbose (IC(50)  = 1674.75 µmol L(-1) ) was used as the reference

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