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Merck
CN

N5885

4-Nitrophenyl α-D-maltoside

glycosidase substrate

Synonym(s):

4-Nitrophenyl a-D-maltopyranoside, 4-Nitrophenyl alpha-D-maltoside

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About This Item

Empirical Formula (Hill Notation):
C18H25NO13
CAS Number:
Molecular Weight:
463.39
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352204
MDL number:
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Quality Level

InChI

1S/C18H25NO13/c20-5-9-11(22)12(23)14(25)18(30-9)32-16-10(6-21)31-17(15(26)13(16)24)29-8-3-1-7(2-4-8)19(27)28/h1-4,9-18,20-26H,5-6H2

SMILES string

O[C@@H]1[C@@H](O)[C@H](O[C@@]2([H])O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)[C@@H](CO)O[C@@H]1OC3=CC=C([N+]([O-])=O)C=C3

InChI key

IAYJZWFYUSNIPN-UHFFFAOYSA-N

assay

≥99% (TLC)

form

powder

solubility

water: 49.00-51.00 mg/mL, clear, colorless to light yellow

storage temp.

−20°C

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

涉药品监管产品
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G Dupuy et al.
Clinical chemistry, 33(4), 524-528 (1987-04-01)
A new chromogenic substrate that is blocked at the nonreducing end, 4,6-benzylidene-alpha-D-4-nitrophenylmaltoheptaoside, is used to determine alpha-amylase (EC 3.2.1.1) activity in serum in a coupled assay with alpha-glucosidase (EC 3.2.1.20) and glucoamylase (EC 3.2.1.3) as auxiliary enzymes. The duration of
M Reyes et al.
Journal of bacteriology, 165(3), 918-922 (1986-03-01)
In wild-type Escherichia coli the activity of the maltose transport system is dependent on a periplasmic maltose-binding protein. It has been possible, however, to isolate mutants in which transport activity is mediated by the membrane components of the system and
[Amylase determination using p-nitrophenylmaltosides].
R Müller-Matthesius
Der Internist, 23(10), 575-578 (1982-10-01)
Reference values for alpha-amylase activity in serum and urine by a new chromogenic amylase method.
S Marcovina et al.
La Ricerca in clinica e in laboratorio, 14(3), 439-442 (1984-07-01)
E H Ajandouz et al.
Biochimica et biophysica acta, 1159(2), 193-202 (1992-09-23)
Isoforms AMY1, AMY2-1 and AMY2-2 of barley alpha-amylase were purified from malt. AMY2-1 and AMY2-2 are both susceptible to barley alpha-amylase/subtilisin inhibitor. The action of these isoforms is compared using substrates ranging from p-nitrophenylmaltoside through p-nitrophenylmaltoheptaoside. The kcat/Km values are

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