A comparative study of aldehyde dehydrogenase and alcohol dehydrogenase activities in crucian carp and three other vertebrates: apparent adaptations to ethanol production

1988 ◽  
Vol 158 (4) ◽  
pp. 479-485 ◽  
Author(s):  
G�ran E. Nilsson
Keyword(s):  
Alcohol Dehydrogenase ◽  
Comparative Study ◽  
Ethanol Production ◽  
Aldehyde Dehydrogenase ◽  
Crucian Carp

scholarly journals Pyruvate-to-ethanol pathway in Entamoeba histolytica

1978 ◽  
Vol 171 (1) ◽  
pp. 225-230 ◽  
Author(s):  
H S Lo ◽  
R E Reeves
Keyword(s):  
Enzyme Activity ◽  
Alcohol Dehydrogenase ◽  
Ethanol Production ◽  
Entamoeba Histolytica ◽  
Aldehyde Dehydrogenase ◽  
Pyruvate Decarboxylase ◽  
Acetyl Coa ◽  
Key Enzyme ◽  
Pyruvate Synthase ◽  
Soluble Enzymes

The pyruvate-to-ethanol pathway in Entamoeba histolytica is unusual when compared with most investigated organisms. Pyruvate decarboxylase (EC 4.1.1.1), a key enzyme for ethanol production, is not found. Pyruvate is converted into acetyl-CoA and CO2 by the enzyme pyruvate synthase (EC 1.2.7.1), which has been demonstrated previously in this parasitic amoeba. Acetyl-CoA is reduced to acetaldehyde and CoA by the enzyme aldehyde dehydrogenase (acylating) (EC 1.2.1.10) at an enzyme activity of 9 units per g of fresh cells with NADH as a reductant. Acetaldehyde is further reduced by either a previously identified NADP+-linked alcohol dehydrogenase or by a newly found NAD+-linked alcohol dehydrogenase at an enzyme activity of 136 units per g of fresh cells. Ethanol is identified as the product of soluble enzymes of amoeba acting on pyruvate or acetyl-CoA. This result is confirmed by radioactive isotopic, spectrophotometric and gas-chromatographic methods.

Alcohol and aldehyde dehydrogenase activity in the stomach and small intestine of rats poisoned with methanol

2001 ◽  
Vol 20 (5) ◽  
pp. 255-258
Author(s):  
L Chrostek ◽  
D Szczepura ◽  
M Szmitkowski ◽  
W Jelski ◽  
J Wierzchowski
Keyword(s):  
Small Intestine ◽  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Aldehyde Dehydrogenase ◽  
Protein Denaturation ◽  
Cell Damage ◽  
Sublethal Dose ◽  
Adh Activity ◽  
Aldehyde Dehydrogenase Activity

The activities of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were measured with fluorogenic naphthaldehydes in the stomach and small intestine homogenates of rats dosed with 6 g methanol/kg bw after 6, 12, 24 h and 2, 5, 7 days. After intoxication with a sublethal dose, the ADH activity measured with these naphthaldehydes andALDH activities in the stomach and small intestine were significantly decreased. This inhibition is stronger in the stomach and probably depends on cell damage and protein denaturation. We conclude that the activity measured with 6-methoxy-2-naphthaldehyde (MONAL-62) may be due to the activity of rat ADH-1 isoenzyme, and the activity detected with 4-methoxy-1-naphthaldehyde (MONAL-41) to the activity of rat ADH-2 isoenzyme.

Alcohol Dehydrogenase Isoenzymes and Aldehyde Dehydrogenase Activity in the Serum of Patients with Non-alcoholic Fatty Liver Disease

2018 ◽  
Vol 38 (7) ◽  
pp. 4005-4009 ◽  
Author(s):  
WOJCIECH JELSKI ◽  
BLANKA WOLSZCZAK-BIEDRZYCKA ◽  
ELŻBIETA ZASIMOWICZ-MAJEWSKA ◽  
KAROLINA ORYWAL ◽  
TADEUSZ WOJCIECH LAPINSKI ◽  
...  
Keyword(s):  
Liver Disease ◽  
Alcohol Dehydrogenase ◽  
Fatty Liver ◽  
Dehydrogenase Activity ◽  
Aldehyde Dehydrogenase ◽  
Fatty Liver Disease ◽  
Alcohol Dehydrogenase Isoenzymes ◽  
Alcoholic Fatty Liver ◽  
Alcoholic Fatty Liver Disease ◽  
Aldehyde Dehydrogenase Activity
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