F4136
Formaldehyde Dehydrogenase (glutathione-dependent) from Candida boidinii
lyophilized powder, 7-20 units/mg protein
Synonym(s):
Formaldehyde Dehydrogenase (Glutathione) from Candida boidinii, Formaldehyde:NAD+ oxidoreductase (glutathione-formylating)
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About This Item
form
lyophilized powder
specific activity
7-20 units/mg protein
composition
Protein, ~10% Lowry
storage temp.
−20°C
Physical form
Lyophilized powder containing phosphate buffer salts and sucrose as stabilizer
Other Notes
One unit will oxidize 1.0 μmole of formaldehyde to formic acid per min at pH 7.5 at 37 °C in the presence of reduced glutathione.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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H Schüte et al.
European journal of biochemistry, 62(1), 151-160 (1976-02-02)
Formaldehyde hydrogenase and formate dehydrogenase were purified 130-fold and 19-fold respectively from Candida boidinii grown on methanol. The final enzyme preparations were homogenous as judged by acrylamide gel electrophoresis and by sedimentation in an ultracentrifuge. The molecular weights of the
Takeshi Haseba et al.
International journal of environmental research and public health, 7(3), 1076-1092 (2010-07-10)
The conventional view is that alcohol metabolism is carried out by ADH1 (Class I) in the liver. However, it has been suggested that another pathway plays an important role in alcohol metabolism, especially when the level of blood ethanol is
M Ben Ali et al.
Biosensors & bioelectronics, 22(12), 2790-2795 (2006-11-14)
A new formaldehyde-selective biosensor was constructed using NAD(+)- and glutathione-dependent recombinant formaldehyde dehydrogenase as a bio-recognition element immobilised on the surface of Si/SiO(2)/Si(3)N(4) structure. Sensor's response to formaldehyde was evaluated by capacitance measurements. The calibration curves obtained for formaldehyde concentration
Wojciech Jelski et al.
Digestive diseases and sciences, 52(2), 531-535 (2007-01-11)
The metabolism of cancer is in many way different than in healthy cells. Increased metabolism of several carcinogenic substances may take place in cancer cells. The one of them was ethanol, that is oxidized by alcohol dehydrogenase (ADH) to high
Wojciech Jelski et al.
Postepy higieny i medycyny doswiadczalnej (Online), 61, 226-230 (2008-03-28)
The human brain contains three classes of alcohol dehydrogenase (ADH) isoenzymes: classes I, III, and IV. These isoenzymes of ADH participate in the metabolism of many biological substances, such as retinol or serotonin. ADH is responsible for the metabolism of
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