scholarly journals Development of an Alcohol Dehydrogenase Biosensor for Ethanol Determination with Toluidine Blue O Covalently Attached to a Cellulose Acetate Modified Electrode

Sensors ◽  
2010 ◽  
Vol 10 (1) ◽  
pp. 748-764 ◽  
Author(s):  
Şenol Alpat ◽  
Azmi Telefoncu
1978 ◽  
Vol 24 (6) ◽  
pp. 873-876 ◽  
Author(s):  
G Jung ◽  
G Férard

Abstract We describe an automated enzymic method for ethanol determination with a centrifugal analyzer (the GEMSAEC) by measuring the rate of the reaction catalyzed by alcohol dehydrogenase and coupled to aldehyde dehydrogenase. The detection limits, reproducibility, and accuracy of the method have been evaluated. It can be applied to whole blood or plasma, with or without previous deproteinization. Our results, compared with those by an automated alcohol dehydrogenase method in the presence of semicarbazide, show an improved linearity, sensitivity, and rapidity of determination.


2004 ◽  
Vol 20 (12) ◽  
pp. 1725-1728 ◽  
Author(s):  
Yanling CHEN ◽  
Junhua YUAN ◽  
Xiuzhong WANG ◽  
Chunxiang TIAN

1978 ◽  
Vol 24 (2) ◽  
pp. 383-385 ◽  
Author(s):  
J Vasiliades ◽  
J Pollock ◽  
C A Robinson

Abstract We describe a case of ethanol and isopropanol ingestion that resulted in coma. The concentration of ethanol and isopropanol was 0.90 and 1.65 g/liter in serum and 3.12 and 5.34 g/liter in gastric contents. With an enzymatic (alcohol dehydrogenase) method for ethanol determination we obtained erroneous analytical results. Because of partial cross reactivity with isopropanol, ethanol concentration was overestimated and total alcohol (i.e., the contribution of isopropanol) was underestimated. This was recognized by measuring serum osmolality. Differences between measured and calculated serum osmolality that are not accounted for by the serum ethanol concentration as determined by an enzymatic ethanol method must be further investigated by specific methods to see if other alcohols are present.


1980 ◽  
Vol 26 (9) ◽  
pp. 1278-1280 ◽  
Author(s):  
J H Eckfeldt ◽  
R T Light

Abstract We describe a rapid, accurate, and precise two-point kinetic assay for ethylene glycol. The method involves use of a standard kit for ethanol determination with yeast alcohol dehydrogenase, and of a centrifugal analyzer. Alcohol dehydrogenase catalyzes the oxidation of ethylene glycol in a trichloroacetic acid-precipitated specimen; the resulting NADH production is monitored at 340 nm. The reaction rate is linear with concentration to 1.5 g of ethylene glycol per liter. Interference from methanol, ethanol, and isopropanol was easily recognized after a 30-min incubation at 100 degrees C. We believe that the method can be readily adaptable to any narrow-bandwidth, stable, temperature-controlled spectrophotometer and so should provide more widely for the prompt assessment of patients in whom ethylene glycol poisoning is suspected.


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