MITOCHONDRIAL MALATE DEHYDROGENASE AND MALIC ENZYME OF A FILARIAL WORM SETARIA DIGITATA: SOME PROPERTIES AND EFFECTS OF DRUGS AND HERBAL EXTRACTS
| Autor: | Mohammed Jameela Banu, Kaliappan Nellaiappan, Subramanian Dhandayuthapani |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Decarboxylation
Setaria Nematode Malic enzyme Malate dehydrogenase General Biochemistry Genetics and Molecular Biology Malate Dehydrogenase Animals Citrate synthase Plants Medicinal biology Plant Extracts Chemistry food and beverages Hydrogen-Ion Concentration Azadirachta NAD biology.organism_classification Mitochondria Kinetics Biochemistry Carboxylation biology.protein Cattle Female Calotropis gigantea |
| Zdroj: | Japanese Journal of Medical Science and Biology. 45:137-150 |
| ISSN: | 1884-2828 0021-5112 |
| DOI: | 10.7883/yoken1952.45.137 |
| Popis: | Mitochondrial malate dehydrogenase (mMDH) and malic enzyme (mME) of a filarial worm Setaria digitata were studied. mMDH exhibited the highest activities in the oxidation and reduction reactions at pH 9.5 and pH 6.2, respectively, while mME did so in the malate decarboxylation reaction at pH 6.8. mME showed no detectable activity on the pyruvate carboxylation direction. The Km values for malate (1.7 mM) and oxaloacetate (0.17 mM) and the ratio of Vmax oxidation: Vmax reduction (2.73) tend to favor the oxaloacetate reduction by mMDH. mME showed a relatively high Km value of 8.3 mM, for malate decarboxylation. A drug, diethylcarbamazine citrate (DEC-C), did not change appreciably the activity of either mMDH or mME, while filarin (a drug of herbal origin) effectively inhibited mMDH. The leaf extracts of Ocimum sanctum, Lawsonia inermis and Calotropis gigantea and leaf and flower extracts of Azadirachta indica were, however, found to inhibit both mMDH and mME. |
| Databáze: | OpenAIRE |
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