N5885
4-Nitrophenyl α-D-maltoside
glycosidase substrate
别名:
4-Nitrophenyl a-D-maltopyranoside, 4-Nitrophenyl alpha-D-maltoside
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关于此项目
经验公式（希尔记法）:
C18H25NO13
化学文摘社编号:
分子量:
463.39
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352204
MDL number:
产品名称
4-Nitrophenyl α-D-maltoside, glycosidase substrate
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
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
涉药品监管产品
此项目有
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
Huanyu Zhuo et al.
The protein journal, 23(6), 379-387 (2004-11-03)
The X-ray structure analysis of a crystal of pig pancreatic alpha-amylase soaked with a rho-nitrophenyl-alpha-D-maltoside (pNPG2) substrate showed a pattern of electron density corresponding to the binding of a rho-nitrophenol unit at subsite -2 of the active site. Binding of
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
[Amylase determination using p-nitrophenylmaltosides].
R Müller-Matthesius
Der Internist, 23(10), 575-578 (1982-10-01)
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