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  • 1
    Electronic Resource
    Electronic Resource
    Kinetic evidence for human liver and stomach aldehyde dehydrogenase-3 representing an unique class of isozymes (1989)
    Springer
    Biochemical genetics 27 (1989), S. 321-331 
    Details
    ISSN: 1573-4927
    Keywords: aldehyde dehydrogenase ; isozyme ; human stomach and liver ; kinetic property
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Substrate and coenzyme specificities of human liver and stomach aldehyde dehydrogenase (ALDH) isozymes were compared by staining with various aldehydes including propionaldehyde, heptaldehyde, decaldehyde, 2-furaldehyde, succinic semialdehyde, and glutamic γ-semialdehyde and with NAD+ or NADP+ on agarose isoelectric focusing gels. ALDH3 isozyme was isolated from a liver via carboxymethyl-Sephadex and blue Sepharose chromatographies and its kinetic constants for various substrates and coenzymes were determined. Consistent with the previously proposed genetic model for human ALDH3 isozymes (Yinet al., Biochem. Genet. 26:343, 1988), a single liver form and multiple stomach forms exhibited similar kinetic properties, which were strikingly distinct from those of ALDH1, ALDH2, and ALDH4 (glutamic γ-semialdehyde dehydrogenase). A set of activity assays using various substrates, coenzymes, and an inhibitor to distinguish ALDH1, ALDH2, ALDH3, and ALDH4 is presented. As previously reported in ALDH1 and ALDH2, a higher catalytic efficiency (V max/K m) for oxidation of long-chain aliphatic aldehydes was found in ALDH3, suggesting that these enzymes have a hydrophobic barrel-shape substrate binding pocket. Since theK m value for acetaldehyde for liver ALDH3, 83 mM, is very much higher than those of ALDH1 and ALDH2, ALDH3 thus represents an unique class of human ALDH isozymes and it appears not to be involved in ethanol metabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554167
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  • 2
    Electronic Resource
    Electronic Resource
    Human stomach alcohol and aldehyde dehydrogenases (ALDH): A genetic model proposed for ALDH III isozymes (1988)
    Springer
    Biochemical genetics 26 (1988), S. 343-360 
    Details
    ISSN: 1573-4927
    Keywords: alcohol dehydrogenase ; aldehyde dehydrogenase ; genetic model ; human stomach ; isozyme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Isozyme phenotypes of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) from human gastroendoscopic as well as surgical gastric biopsies were determined by starch gel electrophoresis and agarose isoelectric focusing. γγ ADH isozymes were expressed predominantly in the mucosal layer of the stomach, whereas ββ isozymes were in the muscular layer. In the 56 gastroendoscopic mucosal biopsies examined, the homozygous ADH3 1-1 phenotype was found in 75% of the samples, and the heterozygous ADH3 2-1 phenotype in 25%. Accordingly, the gene frequencies of the allelesADH 3 1 andADH 3 2 were calculated to be 0.88 and 0.12, respectively. Using a modified agarose isoelectric focusing procedure, gastric ALDH I, ALDH II, and up to five ALDH III forms could be clearly resolved. The ALDH III isozymes accounted for more than 80% of the total ALDH activities in gastric mucosa and exhibitedK m values in the millimolar range for propionaldehyde atpH 9.0. Forty-five percent of the 55 gastroendoscopic biopsies studied lacked ALDH I isozyme. The complex gastric ALDH III isozyme phenotypes seen in these biopsies fall into three patterns. They can be interpreted by a genetic hypothesis, based on a dimeric molecule, in which there are two separate genes,ALDH 3a andALDH 3b, with theALDH 3b locus exhibiting polymorphism. The homozygous phenotypes ALDH3b 1-1 and ALDH3b 2-2 were found to be 4 and 76%, respectively, and the heterozygous ALDH3b 2-1 phenotype 20%, of the total. Therefore, the allele frequencies forALDH 3b 1 andALDH 3b 2 were calculated to be 0.14 and 0.86, respectively. Several lines of biochemical evidence consistent with this genetic model are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554070
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Human stomach alcohol and aldehyde dehydrogenases (ALDH): A genetic model proposed for ALDH III isozymes (1988)
    Springer
    Biochemical genetics 26 (1988), S. 343-360 
    Details
    ISSN: 1573-4927
    Keywords: alcohol dehydrogenase ; aldehyde dehydrogenase ; genetic model ; human stomach ; isozyme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Isozyme phenotypes of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) from human gastroendoscopic as well as surgical gastric biopsies were determined by starch gel electrophoresis and agarose isoelectric focusing. γγ ADH isozymes were expressed predominantly in the mucosal layer of the stomach, whereas ββ isozymes were in the muscular layer. In the 56 gastroendoscopic mucosal biopsies examined, the homozygous ADH3 1-1 phenotype was found in 75% of the samples, and the heterozygous ADH3 2-1 phenotype in 25%. Accordingly, the gene frequencies of the allelesADH 3 1 andADH 3 2 were calculated to be 0.88 and 0.12, respectively. Using a modified agarose isoelectric focusing procedure, gastric ALDH I, ALDH II, and up to five ALDH III forms could be clearly resolved. The ALDH III isozymes accounted for more than 80% of the total ALDH activities in gastric mucosa and exhibitedK m values in the millimolar range for propionaldehyde atpH 9.0. Forty-five percent of the 55 gastroendoscopic biopsies studied lacked ALDH I isozyme. The complex gastric ALDH III isozyme phenotypes seen in these biopsies fall into three patterns. They can be interpreted by a genetic hypothesis, based on a dimeric molecule, in which there are two separate genes,ALDH 3a andALDH 3b, with theALDH 3b locus exhibiting polymorphism. The homozygous phenotypes ALDH3b 1-1 and ALDH3b 2-2 were found to be 4 and 76%, respectively, and the heterozygous ALDH3b 2-1 phenotype 20%, of the total. Therefore, the allele frequencies forALDH 3b 1 andALDH 3b 2 were calculated to be 0.14 and 0.86, respectively. Several lines of biochemical evidence consistent with this genetic model are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02401788
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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