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

Isoelectric focusing (IEF) techniques and spectrophotometric analyses were used to examine the distribution and properties of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) isozymes in ocular tissue of olive and yellow baboons. Cornea extracts exhibited very high specific activities of the 'stomach-specific' ADH and ALDH isozymes (designated ADH-3 and ALDH-III respectively), and were devoid of the major liver and kidney isozymes. Lens extracts exhibited lower activities of ADH-3 and ALDH-III, and also showed significant activity of ALDH-II (the major liver cytosolic isozyme) and a group of 'lens-specific' ALDHs of low isoelectric point. Extracts of baboon retina also exhibited ADH-3 and ALDH-III activities, together with activities of the major liver cytosolic (ALDH-II) and mitochondrial (ALDH-I) isozymes of ALDH; and ADH-5 (or chi-ADH) activity. Evidence was obtained for individual variation of ALDH-III activity in the lens. An electrophoretic variant for ADH-3 indicated genetic identity of the major stomach and ocular ADH isozyme. The catalytic properties of the high specific activity corneal ADH and ALDH isozymes indicated a role in the detoxification of lipid peroxidation by-products.
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PMID:Ocular NAD-dependent alcohol dehydrogenase and aldehyde dehydrogenase in the baboon. 378 Aug 81

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

By comparison of mass spectra from a small cohort of nipple aspiration fluids (NAF), we previously discovered a panel of five candidate breast cancer biomarkers among them an unidentified 4.7 kD peptide BF5. The purposes of the present study were to verify the presence of BF5 in an independent cohort; to determine the protein identity of BF5; and to provide insight into the biology of BF5 production and elevation in tumor-associated NAF. We prospectively collected bilaterally matched NAF from patients with unilateral Stage I/II breast cancer (IBC-31), ductal carcinoma in situ (DCIS-6), atypical ductal hyperplasia (ADH-5), and presumed healthy women who came to routine mammography and had a normal exam (31). Following the consolidation of its cancer-associated expression on SELDI-mass spectrometry, BF5 was isolated by gel electrophoresis and sequenced by tandem mass spectrometry. BF5 was elevated in 15-25% of women with IBC, DCIS, or ADH vs. 0% of controls. This elevation was restricted to the affected breasts. BF5 was identified as 41/42-aa C-terminal peptide of alpha1-antitrypsin (AAT), the principle inhibitor of serine protease neutrophile elastase. The full length AAT showed a consistent expression pattern as C-41/42, and C-41/42 can be generated in vitro by MMP-7 cleavage. In conclusion, elevated C-41/42 is likely the result of elevated AAT synthesis, and the activity of specific MMPs present within the tumor. As other C-terminal fragments of AAT are reported to function as tumor-derived suppressors to the host immune-system, elevated C-41/42 may also be predictive of a poor outcome.
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PMID:A unique proteolytic fragment of alpha1-antitrypsin is elevated in ductal fluid of breast cancer patient. 1990 53