form
lyophilized powder
contains
citrate as stabilizer, lactose as stabilizer
storage temp.
−20°C
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Application
醇脱氢酶可用于合成手性醇的对映体纯的立体异构体。它可用于研究乙醇燃料电池、酒精中毒和药物依赖性。产品 A2529 来自酿酒酵母，是一种用途广泛的不溶性酶。
Biochem/physiol Actions
Sigma 的不溶酶是由可溶性酶与惰性碱反应制得的。这产生了具有原始酶活性的不溶化合物。醇脱氢酶对醇、酮和乙醛具有广泛的底物特异性。
Other Notes
在 pH8.8，25℃ 条件下，一个单位每分钟可将 1.0 μmole 乙醇转化为乙醛。
存储类别
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
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L S al-Kassim et al.
Biochemistry and cell biology = Biochimie et biologie cellulaire, 68(6), 907-913 (1990-06-01)
Alcohol dehydrogenase has been purified from the cell-free preparation of Thermoanaerobium brockii to homogeneity, employing combined DEAE, Sephadex, and affinity chromatographic procedures. The enzyme is tetrameric having subunit molecular weight of 40.4 x 10(3). The purified alcohol dehydrogenase is capable
Nathan C Contino et al.
Journal of the American Society for Mass Spectrometry, 24(1), 101-108 (2012-12-01)
Charge detection mass spectrometry (CDMS) measurements have been performed for cytochrome c and alcohol dehydrogenase (ADH) monomer using a modified cone trap incorporating a cryogenically cooled JFET. Cooling the JFET increases its transconductance and lowers thermal noise, improving the signal
Shuo Zhou et al.
Biotechnology letters, 35(3), 359-365 (2012-11-20)
The gene encoding a novel short-chain alcohol dehydrogenase in the thermophilic bacterium, Carboxydothermus hydrogenoformans, was identified and overexpressed in Escherichia coli. The enzyme was thermally stable and displayed the highest activity at 70 °C and pH 6.0. It preferred NAD(H) over
Xingxing Diao et al.
Drug metabolism and disposition: the biological fate of chemicals, 41(2), 430-444 (2012-11-22)
3-n-Butylphthalide (NBP) is a cardiovascular drug currently used for the treatment of cerebral ischemia. The present study aims to investigate the metabolism, pharmacokinetics, and excretion of NBP in humans and identify the enzymes responsible for the formation of major metabolites.
Kate M Ehrensberger et al.
The Journal of biological chemistry, 288(2), 759-769 (2012-12-12)
In yeast, Adh1 (alcohol dehydrogenase 1) is an abundant zinc-binding protein that is required for the conversion of acetaldehyde to ethanol. Through transcriptome profiling of the Schizosaccharomyces pombe genome, we identified a natural antisense transcript at the adh1 locus that
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