Detoxification of cyclophosphamide by human aldehyde dehydrogenase isozymes
| Autor: | U von Eitzen, H. W. Goedde, Doris Meier-Tackmann, D.P. Agarwal |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Cancer Research
Lung Neoplasms Cyclophosphamide Aldehyde dehydrogenase Adenocarcinoma Isozyme Substrate Specificity chemistry.chemical_compound Mafosfamide Tumor Cells Cultured medicine Humans chemistry.chemical_classification biology Aldophosphamide Pharyngeal Neoplasms Metabolism Aldehyde Dehydrogenase In vitro Isoenzymes Enzyme Liver Oncology chemistry Biochemistry Gastric Mucosa Inactivation Metabolic biology.protein Phosphoramide Mustards Isoelectric Focusing Oxidation-Reduction medicine.drug |
| Zdroj: | Cancer Letters. 76:45-49 |
| ISSN: | 0304-3835 |
| Popis: | In in vitro studies, no turnover of aldophosphamide and mafosfamide was observed with the tumor-specific aldehyde dehydrogenase 3 isozyme (ALDH3) isolated from human stomach mucosa as well as from lung (A549) and pharynx (UMSCC2) carcinoma cell lines. Only the human liver cytosolic ALDH preparation (ALDH1) showed any significant oxidation of aldophosphamide and mafosfamide. |
| Databáze: | OpenAIRE |
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