对硝基苯基麦芽五糖结构式
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常用名 | 对硝基苯基麦芽五糖 | 英文名 | 4-Nitrophenyl α-D-maltopentaoside |
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| CAS号 | 66068-38-0 | 分子量 | 949.812 | |
| 密度 | 1.8±0.1 g/cm3 | 沸点 | 1259.3±65.0 °C at 760 mmHg | |
| 分子式 | C36H55NO28 | 熔点 | N/A | |
| MSDS | 中文版 美版 | 闪点 | 715.4±34.3 °C | |
| 符号 |
GHS07 |
信号词 | Warning |
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Selective α-glucosidase substrates and inhibitors containing short aromatic peptidyl moieties.
Bioorg. Med. Chem. Lett. 21 , 2441-4, (2011) 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 ... |
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Subsite mapping of porcine pancreatic alpha-amylase I and II using 4-nitrophenyl-alpha-maltooligosaccharides.
Carbohydr. Res. 268(2) , 267-77, (1995) The catalytic efficiency (kcat/Km) and the cleaved bond distribution for the nitrophenylated maltooligosaccharides, p-NPGlcn (2 < or = n < or = 7) hydrolysed by porcine pancreatic alpha-amylase isozymes I and II were determined. The subsite affinities (Ai) we... |
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New type of starch-binding domain: the direct repeat motif in the C-terminal region of Bacillus sp. no. 195 alpha-amylase contributes to starch binding and raw starch degrading.
Biochem. J. 350 Pt 2 , 477-84, (2000) 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-res... |
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Enzymatic synthesis of p-nitrophenyl 4(5)-O-beta-D-galactosyl-alpha-maltopentaoside as a substrate for human alpha-amylases.
Anal. Biochem. 202(1) , 61-7, (1992) 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... |
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Evaluation of silyl-blocked p-nitrophenylmaltoheptaoside as a substrate for alpha-amylase reagents.
Clin. Chem. 39(1) , 112-8, (1993) 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-nitrophenylmaltoh... |
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Catalytic properties of IgMs with amylolytic activity isolated from patients with multiple sclerosis.
Med. Sci. Monit. 10(8) , BR273-80, (2004) 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 ac... |