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N1519

Sigma-Aldrich

4-Nitrophenyl α-D-maltopentaoside

≥98%

Synonym(s):

4-Nitrophenyl α-D-penta-(1→4)-glucopyranoside

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About This Item

Empirical Formula (Hill Notation):
C36H55NO28
CAS Number:
66068-38-0
Molecular Weight:
949.81
Beilstein/REAXYS Number:
4839501
MDL number:
MFCD00065706
UNSPSC Code:
12352204
PubChem Substance ID:
24897499

assay

≥98%

form

powder

solubility

water: 50 mg/mL, clear, colorless to light yellow

storage temp.

−20°C

SMILES string

OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O[C@@H]2CO)O[C@H]3[C@H](O)[C@@H](O)[C@H](O[C@@H]3CO)O[C@H]4[C@H](O)[C@@H](O)[C@H](O[C@@H]4CO)O[C@H]5[C@H](O)[C@@H](O)[C@H](O[C@@H]5CO)Oc6ccc(cc6)[N+]([O-])=O)[C@H](O)[C@@H](O)[C@@H]1O

InChI

1S/C36H55NO28/c38-5-12-17(43)18(44)23(49)33(57-12)62-29-14(7-40)59-35(25(51)20(29)46)64-31-16(9-42)61-36(27(53)22(31)48)65-30-15(8-41)60-34(26(52)21(30)47)63-28-13(6-39)58-32(24(50)19(28)45)56-11-3-1-10(2-4-11)37(54)55/h1-4,12-36,38-53H,5-9H2/t12-,13-,14-,15-,16-,17-,18+,19-,20-,21-,22-,23-,24-,25-,26-,27-,28-,29-,30-,31-,32+,33-,34-,35-,36-/m1/s1

InChI key

YXGBAQKCCMQLGH-MYPSSPKESA-N

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Substrates

Chromogenic substrate for α-amylase.

Certificates of Analysis (COA)

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α-Amylase from human saliva Type XIII-A, lyophilized powder, 300-1,500 units/mg protein

Sigma-Aldrich

A1031

α-Amylase from human saliva

T Usui et al.
Analytical biochemistry, 202(1), 61-67 (1992-04-01)
Enzymatic modification at the nonreducing end D-glucosyl residue of p-nitrophenyl alpha-maltopentaoside was developed by using the transglycosylation of beta-D-galactosidase from Bacillus circulans. The enzyme regioselectively synthesized p-nitrophenyl 4(5)-O-beta-D-galactosyl-alpha-maltopentaoside (a yield of 12.0% based on the amount of p-nitrophenyl alpha-maltopentaoside added)
Dina R Ivanen et al.
Medical science monitor : international medical journal of experimental and clinical research, 10(8), BR273-BR280 (2004-07-28)
Recently, amylolytic activity was detected in IgMs isolated from the sera of the patients with multiple sclerosis. All purified samples of IgM were electrophoretically homogenous and did not contain any co-purified a-amylase and a-glucosidase activities, in accordance with a set
C S Elbin et al.
Clinical chemistry, 39(1), 112-118 (1993-01-01)
We describe a reagent for measuring alpha-amylase (EC 3.2.1.1) activity in serum with use of a thexyldimethylsilyl ether of p-nitrophenyl-alpha-D-maltoheptaoside (SB7) as substrate. This substrate differs from Genzyme's benzylidene-blocked p-nitrophenylmaltoheptaoside substrate (B-PNPG7). The reagent, optimized for the characteristics of the
J Sumitani et al.
The Biochemical journal, 350 Pt 2, 477-484 (2000-08-19)
The alpha-amylase from Bacillus sp. no. 195 (BAA) consists of two domains: one is the catalytic domain similar to alpha-amylases from animals and Streptomyces in the N-terminal region; the other is the functionally unknown domain composed of an approx. 90-residue
Sangeun Park et al.
Bioorganic & medicinal chemistry letters, 21(8), 2441-2444 (2011-03-15)
We constructed a library of sugar-dipeptide conjugate to find out the best complementary against hydrophobic pocket of α-glucosidase. The best substrate showed 150-fold improved K(m) value relative p-acetaminophenyl-α-D-glucopyranoside for α-glucosidase from Bacillus stearothermophillus. Using information from the complementary, we synthesized
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