Purification and properties of ostrich heart malate dehydrogenases
| Autor: | Kitto Gb |
|---|---|
| Rok vydání: | 1967 |
| Předmět: |
Electrophoresis
Oxaloacetates Malate dehydrogenase Catalysis Poultry Birds Malate Dehydrogenase Oxidoreductase Animals Citrate synthase Fluorometry Amino Acids chemistry.chemical_classification biology Myocardium Complement Fixation Tests General Medicine Molecular biology Mitochondria Amino acid Molecular Weight Kinetics Enzyme chemistry Biochemistry Homogeneous biology.protein Crystallization |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Enzymology. 139:16-23 |
| ISSN: | 0005-2744 |
| DOI: | 10.1016/0005-2744(67)90108-8 |
| Popis: | The supernatant form of malate dehydrogenase l -malate; DPN oxidoreductase, EC 1.1.1.37 has been purified from the heart of a Masai ostrich ( Struthio camelus ). The enzyme was crystallized and was found to be homogeneous on ultracentrifugal analysis, having a s 20,w value of 3.8. The properties of this enzyme have been compared with the properties of partially purified ostrich mitochondrial malate dehydrogenase and with crystalline chicken supernatant and mitochondrial malate dehydrogenases. Both ostrich enzymes have properties very similar to their counterparts in chicken. The amino acid compositions of ostrich and chicken supernatant malate dehydrogenases are strikingly similar. |
| Databáze: | OpenAIRE |
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