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N5885

Sigma-Aldrich

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:
17400-77-0
Molecular Weight:
463.39
MDL number:
MFCD00036769
UNSPSC Code:
12352204
PubChem Substance ID:
24897757
NACRES:
NA.32

Quality Level

200

Assay

≥99% (TLC)

form

powder

solubility

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

storage temp.

−20°C

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

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

InChI key

IAYJZWFYUSNIPN-UHFFFAOYSA-N

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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[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)
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
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
H Yamashita et al.
Biochemistry and molecular biology international, 35(1), 79-85 (1995-01-01)
The effect of chemical modification of lysine residues on the activity of porcine pancreatic alpha-amylase (PPA) was examined, using p-nitrophenyl-alpha-D-maltoside, p-nitrophenyl-alpha-D-maltotrioside, phenyl-alpha-D-maltoside and phenyl-alpha-D-maltotrioside as substrates. Chemical modification of PPA with trinitrobenzenesulfonic acid enhanced the kcat/Km values for p-nitrophenyl substrates
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