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Publication Detail
Chromosome assignment, biochemical and immunological studies on a human aldehyde dehydrogenase, ALDH3.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Santisteban I, Povey S, West LF, Parrington JM, Hopkinson DA
  • Publication date:
  • Pagination:
    87, 100
  • Journal:
    Ann Hum Genet
  • Volume:
  • Issue:
  • Status:
  • Country:
  • Print ISSN:
  • Language:
  • Keywords:
    Aldehyde Dehydrogenase, Animals, Chromosome Mapping, Chromosomes, Human, 16-18, Electrophoresis, Starch Gel, Fetus, Humans, Hybrid Cells, Isoenzymes, Liver, Lung, Precipitin Tests, Rats, Species Specificity, Stomach, Substrate Specificity, Tissue Distribution
The biochemical properties of ALDH isozymes have been examined in human tissues and one set, designated ALDH3, has been studied in detail. These components occur at highest levels in lung and stomach, but were not expressed in fetal tissues, or in blood, hair roots and fibroblasts. The ALDH3 isozymes show optimal activity with benzaldehyde and can use either NAD or NADP as cofactor. Antiserum against a partially purified ALDH3, from stomach, selectively precipitates this isozyme from human tissues and selectively recognizes an homologous component in the rat. Human and rodent ALDH3 were not immunoprecipitated by anti-ALDH1 or anti-ALDH2 antisera. High levels of expression were found in human-rodent hybrids, constructed using rat hepatoma cells, and these hybrids were used to assign the human ALDH3 gene to chromosome 17.
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