Electrophoretic and biochemical studies of human aldehyde dehydrogenase isozymes in various tissues
| Autor: | Agarwal Dp, Goedde Hw, S. Harada |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Hot Temperature
Electrophoresis Starch Gel Aldehyde dehydrogenase Isozyme General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound Drug Stability medicine Humans Tissue Distribution General Pharmacology Toxicology and Pharmaceutics chemistry.chemical_classification biology Isoelectric focusing Propionaldehyde General Medicine Aldehyde Oxidoreductases Molecular biology Isoenzymes Kinetics Starch gel electrophoresis Enzyme Isoelectric point chemistry Biochemistry Disulfiram biology.protein Isoelectric Focusing medicine.drug |
| Zdroj: | Life Sciences. 26:1773-1780 |
| ISSN: | 0024-3205 |
| DOI: | 10.1016/0024-3205(80)90577-9 |
| Popis: | Four major ALDH isozymes have been identified in human tissues using starch gel electrophoresis and isoelectric focusing. The isozyme bands have been termed as ALDH I, II, III and IV according to their decreasing electrophoretic migration and increasing isoelectric point. The isozymes have been partially purified via preparative isoelectric focusing. Kinetic characteristics of ALDH I and II were found to be quite similar to ALDH enzyme 2 and enzyme 1 described earlier by Greenfield and Pietruszko (Biochem Biophys Acta, 483 35–45 1977). ALDH III and IV showed a very high Km for propionaldehyde (1.0–1.5 mM at pH 9.5) and were not inhibited by disulfiram at pH 9.5. A variant phenotype of ALDH which lacked in isozyme I was detected in various tissues from Japanese individuals. Comparative kinetic properties of normal and variant enzyme are given. |
| Databáze: | OpenAIRE |
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