Simultaneous single-step purification of thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri
| Autor: | Maris G.N. Hartmanis, Mark X. Sliwkowski |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Chemical Phenomena
Biophysics Dehydrogenase Biology Biochemistry Clostridium Acetyltransferases Acetyl-CoA C-Acetyltransferase Amino Acids Molecular Biology chemistry.chemical_classification Chromatography Thiolase Clostridium kluyveri Isoelectric focusing 3-Hydroxyacyl CoA Dehydrogenases Cell Biology biology.organism_classification Chromatography Ion Exchange 3-Hydroxyacyl-CoA Dehydrogenase Chemistry Enzyme chemistry Acetyl-CoA C-acetyltransferase lipids (amino acids peptides and proteins) Electrophoresis Polyacrylamide Gel Isoelectric Focusing |
| Zdroj: | Analytical biochemistry. 141(2) |
| ISSN: | 0003-2697 |
| Popis: | Thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri were purified by ion-exchange chromatography to near homogeneity in a simultaneous, single-step procedure. The yield of both enzymes was greater than 80%. Thiolase was purified approximately 8-fold with sp act 115 units/mg, whereas 3-hydroxybutyryl-CoA dehydrogenase was purified 14-fold with sp act 292 units/mg. Isoelectric points of the enzymes are 7.7 for thiolase and 7.8 for 3-hydroxybutyryl-CoA dehydrogenase. Milligram quantities of each of these enzymes are readily obtained from this fatty acid-producing organism. |
| Databáze: | OpenAIRE |
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