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Merck
CN

N5885

Sigma-Aldrich

4-Nitrophenyl α-D-maltoside

glycosidase substrate

别名:

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

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About This Item

经验公式(希尔记法):
C18H25NO13
CAS号:
分子量:
463.39
MDL编号:
UNSPSC代码:
12352204
PubChem化学物质编号:
NACRES:
NA.32

质量水平

方案

≥99% (TLC)

表单

powder

溶解性

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

储存温度

−20°C

SMILES字符串

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

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

法规信息

监管及禁止进口产品

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分析证书(COA)

Lot/Batch Number

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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)
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
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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