Purification and properties of Drosophila virilis Texmelucan L-glycerol-3-phosphate dehydrogenase
| Autor: | G B Kitto, M S McReynolds, M Seng |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
Insecta
Physiology Dehydrogenase Glycerolphosphate Dehydrogenase Biochemistry Drug Stability Species Specificity Animals Molecular Biology chemistry.chemical_classification biology Molecular mass Temperature General Medicine Hydrogen-Ion Concentration biology.organism_classification Molecular biology Drosophila virilis Gryllus Molecular Weight Electrophoresis Kinetics Enzyme Glycerol-3-phosphate dehydrogenase chemistry Specific activity Drosophila Rabbits |
| Zdroj: | Comparative biochemistry and physiology. B, Comparative biochemistry. 53(2) |
| ISSN: | 0305-0491 |
| Popis: | 1. 1. Extramitochondrial l -glycerol-3-phosphate dehydrogenase has been purified approximately 60-fold from Drosophila viritis Texmelucan. The enzyme was pure as judged by electrophoresis and crystallization to constant specific activity. 2. 2. The Drosophila enzyme has been compared with the corresponding enzymes from the cricket Gryllus gryllus and from skeletal muscle of the rabbit, Oryctolagus cuniculus . The three enzymes were each found to have molecular weights of approximately 67,000 but they differ in pH optima, thermolability and electrophoretic mobility. |
| Databáze: | OpenAIRE |
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