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)

Electrophoretic and activity variation of the stomach and ocular isozyme of aldehyde dehydrogenase (designated AHD-4) was observed between C57BL/6J and SWR/J inbred strains of mice. The phenotypes were inherited in a normal mendelian fashion, with two alleles at a single locus (Ahd-4) showing codominant expression. The alleles assorted independently of those at Adh-3 [encoding the stomach and ocular isozyme of alcohol dehydrogenase (ADH-C2)] on chromosome 3. Three chromosome 11 markers, hemoglobin alpha-chain (Hba), trembler (Tr), and rex (Re), were used in backcross analyses which established that Ahd-4 is closely linked to trembler. The distribution patterns for stomach and ocular AHD-4 phenotypes were examined among SWXL recombinant inbred mice, and those for stomach and ocular ADH-C2 among BXD recombinant inbred strains. The data provided evidence for the genetic identity of stomach and ocular ADH-C2 and of stomach and ocular AHD-4.
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PMID:Genetics of ocular NAD+-dependent alcohol dehydrogenase and aldehyde dehydrogenase in the mouse: evidence for genetic identity with stomach isozymes and localization of Ahd-4 on chromosome 11 near trembler. 340 74

A monoclonal antibody (mHADH1) against alcohol dehydrogenase was found to cross-react with an abundant protein in human serum. This cross-reacting material was identified unambiguously as the third component of complement (C3), probably part of the alpha-chain, by immunoblotting and immunoprecipitation experiments. The known ADH epitope, HVLPF, recognized by the monoclonal antibody is not, however, present in the C3 sequence.
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PMID:A monoclonal antibody to alcohol dehydrogenase cross-reacts with human complement component C3. 769 Nov 12

The amino-acid sequences of human alcohol dehydrogenase alpha-chain (ADH1) were analysed according to two-, three- and four-amino-acid sequences. The measured frequencies and probabilities were compared with the predicted frequencies and probabilities. Of 373 two-amino-acid sequences in the ADH1, 92 (24.665%) and 32 (8.579%) sequences can be explained by the predicted frequencies and probabilities according to a purely random mechanism. Of 191 non-appearing two-amino-acid sequences in the ADH1, 119 (62.304%) and 52 (27.225%) sequences can be explained by the predicted frequencies and probabilities according to a purely random mechanism. Of 373 measured first-order Markov transition probabilities for the second amino acid in two-amino-acid sequences, three (0.804%) probabilities match the predicted conditional probabilities and therefore can be explained by a purely random mechanism. No more-than-two-amino-acid sequences can be explained by a purely random mechanism.
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PMID:Frequency and Markov chain analysis of the amino-acid sequence of human alcohol dehydrogenase alpha-chain. 1086 52