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

1. Starch gel electrophoresis of adult shrew (Suncus murinus) liver extracts revealed five forms of alcohol dehydrogenase (ADH 1-5) and four of them were purified. 2. ADH-4 and ADH-5 resemble human class I ADH in terms of electrophoretic mobility, substrate specificity and sensitivity to pyrazole inhibition. 3. ADH-2 does not belong to any of the three classes of human ADHs but rather with catalytic properties similar to those of the class B ADH found in guinea pig liver. 4. ADH-1 prefers secondary alcohol over primary alcohol substrates and between the enantiomers tested, the enzyme favors the S isomers.
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PMID:Isolation and characterization of shrew (Suncus murinus) liver alcohol dehydrogenases. 266 17

Isoelectric focusing and cellulose acetate electrophoresis were used to examine the multiplicity, tissue distribution, and variability of alcohol dehydrogenase (ADH) among baboons, a primate species used as a model for research on alcohol metabolism and alcohol-induced liver pathology. Five major ADH isozymes were resolved and distinguished on the basis of their isoelectric points, tissue distributions, relative activities with alcohol substrates, and sensitivities to inhibition with 4-methyl pyrazole. ADH-1 and ADH-2 exhibited class I kinetic properties and were observed in high activity in kidney and liver extracts, respectively. ADH-3 showed class II kinetic properties, exhibiting high activity in stomach extracts, and was widely distributed in extracts of other baboon tissues, including kidney, esophagus, heart, testis, brain, and male sex accessory tissues. ADH-4 also showed class II ADH properties but was found only in liver (similar to human "pi-ADH"). ADH-5 exhibited class III ADH kinetic properties, being inactive with ethanol up to 0.5 M (similar to human "chi-ADH") and was distributed widely in baboon tissue extracts. Major activity variation was observed for liver ADH-4 between different animals. An electrophoretic variant for ADH-3 was observed for the enzyme in stomach, kidney, and testis extracts, and activity variation existed for this isozyme in kidney extracts. It is apparent that baboon ADH shares a number of features with the human ADH phenotype; however, several species-specific differences were observed, particularly for the liver and kidney class I isozymes and for stomach ADH.
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PMID:Alcohol dehydrogenase isozymes in baboons: tissue distribution, catalytic properties, and variant phenotypes in liver, kidney, stomach, and testis. 354 15

According to the nomenclature of Vallee and Bazzone [1983] for mammalian alcohol dehydrogenase (ADH) isozymes, baboon ADHs comprise three major classes of activity, which were distinguished according to the following properties: Class I ADHs. These isozymes exhibited low-Km characteristics with ethanol as substrate, high isoelectric points (8.5-9.3), and sensitivity to 5 mM 4-methyl pyrazole inhibition, and were the major liver (ADH-2) and kidney (ADH-1) isozymes in the baboon. Class II ADHs. These isozymes showed high-Km values for ethanol, neutral isoelectric points (7.7 for the liver ADH-4 [pi-ADH] and 7.2 for the major stomach ADH [ADH-3], respectively), and were insensitive to inhibition with 5 mM 4-methyl pyrazole. Class III ADH. This enzyme was characterized by its inactivity with ethanol as substrate (up to 0.5 M), insensitivity to 4-methyl pyrazole inhibition, preference for medium-chain-length alcohols as substrate (trans-2-hexen-1-ol was routinely used in this study), and an isoelectric point (6.5) similar to that of the human liver chi-ADH (pI 6.4). Major activity variation of the liver pi-ADH (ADH-4) isozyme was observed among the 114 liver samples examined, with 34 percent exhibiting a null (or low-activity) phenotype. An electrophoretic variant phenotype for the major class II stomach isozyme (ADH-3) was also found in the population studied. The baboon was used as a model for studying alcohol-induced changes in liver ADH phenotype following chronic alcohol consumption. Prepuberal male baboons were pair-fed nutritionally adequate liquid diets containing ethanol (50 percent of calories) or isocaloric carbohydrates, and liver ADH isozyme patterns from biopsy samples were monitored for 20 weeks. Dramatic decreases in class II liver ADH activity (ADH-4, or pi-ADH) were observed within 4 weeks after the start of alcohol feeding, and a shift in liver class I isozymes was found during the later stages of alcohol consumption. These changes during chronic alcohol consumption may be adaptations of the liver: these include reduced capacity of the major ADH pathway and increased ethanol oxidation by the microsomal ethanol oxidizing system and possibly by peroxisomal catalase.
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PMID:Baboon alcohol dehydrogenase isozymes: phenotypic changes in liver following chronic consumption of alcohol. 361 May 85

Alcohol dehydrogenase (ADH; EC 1.1.1.1) isozymes were investigated in tissue of Cereus peruvianus cultured in different concentrations of 2,4-dichlorophenoxyacetic acid (2,4-D) and kinetin. Five ADH isozymes were detected in starch gel and showed different patterns in seeds, seedlings, calli cultured at 32 and 22 degrees C, and plants regenerated from calli cultured in three 2,4-D and kinetin combinations. Four phenotypes formed by different combinations of ADH-2, ADH-3, ADH-4, and ADH-5 were detected in calli cultured at 32 degrees C and in plants regenerated from calli. ADH-1 isozyme was detected only in calli subcultured for 1 or 2 weeks at 22 degrees C and was indicated as a marker of stress conditions that affect the growth of C. peruvianus callus tissues in culture. ADH phenotypes with either a higher or a lower number of isozymes were detected in different proportions in the callus tissues cultured in media containing different 2,4-D and kinetin ratios. ADH isozyme patterns were found to be sensitive markers at the highest kinetin concentration or at high kinetin/2,4-D ratios. The results indicate a high correlation between the ADH isozyme patterns and the capacity for regeneration. Thus, ADH isozymes are indicated as good biochemical markers and as a powerful tool for monitoring studies of C. peruvianus callus cultures.
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PMID:Alcohol dehydrogenase (EC 1.1.1.1) isozymes as markers at 2,4-dichlorophenoxyacetic acid x kinetin combinations in callus cultures of Cereus peruvianus (Cactaceae). 799 74