Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.1 (alcohol dehydrogenase)
 9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Both class I and class II alcohol dehydrogenase (ADH) activities are present in human serum. The contribution of each class can be measured using two class-specific, fluorogenic substrates, 4-methoxy-1-naphthaldehyde and 6-methoxy-2-naphthaldehyde. The former is highly selective for class I isozymes, especially those containing alpha or gamma subunits, whereas class II (pi) ADH preferentially reduces the latter. Selective inhibition of class I ADH by 4-methylpyrazole further increases the specificity. Specificity, accuracy, and precision of the assay for serum measurements have been determined. The activity of class I ADH in normal human serum is below the limit of detection of this method, i.e., less than 1.0 nM/min. The activity of class II ADH in normal individuals is 15 +/- 5 nM/min. In some patients values as high as 2100 nM/min are observed for class I, but in all instances, the amount of class II found was higher than that of class I ADH.
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PMID:Determination of human serum alcohol dehydrogenase using isozyme-specific fluorescent substrates. 161 24

Two new fluorogenic substrates for human alcohol dehydrogenase (ADH), 4-methoxy-1-naphthaldehyde (IA) and 6-methoxy-2-napthaldehyde (IIA), are described. The 2-naphthaldehyde derivative fluoresces in aqueous media with a quantum yield of 0.22 with an emission maximum at 450 nm, but the 1-naphthaldehyde shows only weak fluorescence. The corresponding alcohol reduction products, 4-methoxy-1-naphthalenemethanol (IB) and 6-methoxy-2-naphthalenemethanol (IIB), exhibit fluorescence in the near uv region with quantum yields of 0.36 and 0.26, respectively. The Km values for the individual homogenous class I ADH isozymes, with the above naphthaldehydes as substrates, range from 0.35 to 11.5 microM. The kappa cat values range from 70 to 610 min-1 and are thus comparable to those for the best ADH substrates. Except for the beta 1 beta 1 isozyme, IA is the preferred substrate for class I ADH isozymes while IIA is rapidly reduced by class II (pi-ADH). The sensitivity and specificity of the enzymatic assay with IA as substrate are demonstrated and provide the basis for the determination of class I ADH activity in human serum.
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PMID:Fluorometric assays for isozymes of human alcohol dehydrogenase. 272 80

We examined the activities of class I and II alcohol dehydrogenase isoenzymes in the sera of patients with viral hepatitis using the fluorogenic substrates 4-methoxy-1-naphthaldehyde for class I and 6-methoxy-2-naphthaldehyde for class II. It was found that serum activities of class I and II alcohol dehydrogenase isoenzymes over the course of five weeks of hospitalisation were higher than those of controls. The greatest increase in activities was found at the onset of disease, exceeding the mean control value by about 30 fold for class I and 4 fold for class II. These activities were lower than that of aminotransferase but higher than those for lactate dehydrogenase, alkaline phosphatase and gamma-glutamyltransferase. Thereafter, the activity of alcohol dehydrogenase isoenzymes gradually decreased, but did not reach the values of the control groups in the last period of the study. Activities of class I and II alcohol dehydrogenase isoenzymes correlated well with those of alanine and aspartate aminotransferase and lactate dehydrogenase in the first weeks of illness. These results clearly demonstrate that especially the activity of class I alcohol dehydrogenase isoenzyme measured by a fluorimetric method can be a useful marker of liver cell damage in the course of viral hepatitis.
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PMID:Serum class I and II alcohol dehydrogenase activity during the course of viral hepatitis. 862 59

We examined the activity of class I and II of alcohol dehydrogenase isoenzymes in the sera of patients with viral hepatitis using fluorogenic substrates, 4-methoxy-1-naphthaldehyde for class I and 6-methoxy-2-naphthaldehyde for class II. It was found that serum activities of class I and II of alcohol dehydrogenase isoenzymes during five weeks of hospitalisation were higher than that of control. The greatest increase in activities was found at the onset of disease, and exceeded the mean control value about 30 times for class I and 4 times for class II. These were lower than the aminotransferase activities but higher than the activity of lactate dehydrogenase, alkaline phosphatase and gamma-glutamyltransferase. In the following periods of investigation the activity of alcohol dehydrogenase isoenzymes gradually decreased, but did not reach the values of the control groups in the last period of the study. Activity of class I and II of alcohol dehydrogenase isoenzymes showed a good correlation with alanine and aspartate aminotransferase and lactate dehydrogenase in the first weeks of the illness. These results clearly demonstrate that particularly the activity of class I of alcohol dehydrogenase isoenzymes measured by a fluorimetric method can be a useful marker of liver cell damage in the course of viral hepatitis.
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PMID:Human serum alcohol dehydrogenase isoenzymes as a markers of liver injury during viral hepatitis. 902 May 38

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 and ALDH 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.
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PMID:Alcohol and aldehyde dehydrogenase activity in the stomach and small intestine of rats poisoned with methanol. 1147 58

Human gastric mucosa contains three classes of alcohol dehydrogenase (ADH) isoenzymes: I, III, and IV. Various factors have been found to influence gastric ADH activity. One of them is Helicobacter pylori infection, which is associated with gastric mucosal injury and leads to a decrease in gastric ADH activity. The aim of the study was to assess the effect of H. pylori infection on the serum activity of ADH isoenzymes. Serum samples were taken from 35 patients with H. pylori infection and from 35 healthy subjects. For measurement of class I isoenzyme activity we employed the fluorometric method, with class-specific fluorogenic substrate (4-methoxy-1-naphthaldehyde). The activities of class III and IV ADH isoenzymes were measured by the photometric method with formaldehyde and with m-nitrobenzaldehyde as substrate, respectively. Total activity of ADH was measured by a photometric method with p-nitrosodimethylaniline. The total activities of ADH and class IV isoenzyme were significantly higher in sera of patients with H. pylori infection compared to healthy subjects. The serum activity of other tested isoenzymes of ADH did not differ significantly between infected and noninfected groups. We conclude that H. pylori infection of gastric mucosa is reflected in the serum by a significant increase in class IV and total ADH activity.
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PMID:Alcohol dehydrogenase (ADH) isoenzyme activity in the sera of patients with Helicobacter pylori infection. 1740 75