Ethanol oxidation and the inhibition by drugs in human liver, stomach and small intestine: Quantitative assessment with numerical organ modeling of alcohol dehydrogenase isozymes

2016 ◽  
Vol 258 ◽  
pp. 134-141 ◽  
Author(s):  
Yu-Chou Chi ◽  
Shou-Lun Lee ◽  
Ching-Long Lai ◽  
Yung-Pin Lee ◽  
Shiao-Pieng Lee ◽  
...  
Keyword(s):  
Small Intestine ◽  
Alcohol Dehydrogenase ◽  
Human Liver ◽  
Quantitative Assessment ◽  
Ethanol Oxidation ◽  
Organ Modeling

scholarly journals H8Zn(c)2 and Zn(c)2Co(n)2 human liver alcohol dehydrogenase

1988 ◽  
Vol 173 (2) ◽  
pp. 281-285 ◽  
Author(s):  
Grazyna FORMICKA-KOZLOWSKA ◽  
Helga SCHNEIDER-BERNLOHR ◽  
Jean-Pierre WARTBURG ◽  
Michael ZEPPEZAUER
Keyword(s):  
Alcohol Dehydrogenase ◽  
Human Liver ◽  
Liver Alcohol Dehydrogenase

Physical and enzymatic properties of a class III isozyme of human liver alcohol dehydrogenase: .chi.-ADH

Biochemistry ◽  
1984 ◽  
Vol 23 (10) ◽  
pp. 2193-2199 ◽  
Author(s):  
Fred W. Wagner ◽  
Xavier Pares ◽  
Barton Holmquist ◽  
Bert L. Vallee
Keyword(s):  
Alcohol Dehydrogenase ◽  
Human Liver ◽  
Enzymatic Properties ◽  
Class Iii ◽  
Liver Alcohol Dehydrogenase

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.

General base catalysis in a glutamine for histidine mutant at position 51 of human liver alcohol dehydrogenase

Biochemistry ◽  
1991 ◽  
Vol 30 (4) ◽  
pp. 1062-1068 ◽  
Author(s):  
Torsten Ehrig ◽  
Thomas D. Hurley ◽  
Howard J. Edenberg ◽  
William F. Bosron
Keyword(s):  
Alcohol Dehydrogenase ◽  
Human Liver ◽  
Base Catalysis ◽  
General Base ◽  
Liver Alcohol Dehydrogenase

Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes

Biochemistry ◽  
1988 ◽  
Vol 27 (4) ◽  
pp. 1132-1140 ◽  
Author(s):  
Rudolf Kaiser ◽  
Barton Holmquist ◽  
John Hempel ◽  
Bert L. Vallee ◽  
Hans Jörnvall
Keyword(s):  
Alcohol Dehydrogenase ◽  
Human Liver ◽  
Structural Type ◽  
Class Ii ◽  
Class I ◽  
Class Iii ◽  
Liver Alcohol Dehydrogenase
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