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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)

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I S Lukomskaya et al.
Clinica chimica acta; international journal of clinical chemistry, 244(2), 145-154 (1996-01-31)
The method of assay of neutral alpha-glucosidase from human kidney and urine using beta-maltosides (p-nitrophenyl-beta-D-maltoside [NP-beta-D-maltoside], 2-chloro-4-nitrophenyl-beta-D-maltoside]) [CNP-beta-D-maltoside] and 4-methylumbelliferyl-beta-D-maltosides ([MU-beta-D-maltoside]) as substrates and beta-glucosidase as an auxiliary enzyme is proposed. All three beta-maltosides are suitable substrates for the determination
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
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)
[Amylase determination using p-nitrophenylmaltosides].
R Müller-Matthesius
Der Internist, 23(10), 575-578 (1982-10-01)
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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