Purification and characterization of limonoate dehydrogenase from Rhodococcus fascians.
Limonoate dehydrogenase from Rhodococcus fascians has been purified to electrophoretic homogeneity by a procedure that consists of ion-exchange, hydrophobic, and affinity chromatography. The native enzyme has a molecular mass of around 128,000 Da and appears to be composed of four similar subunits (...
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| 出版年: | Appl Environ Microbiol |
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| 主要な著者: | , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American Society for Microbiology (ASM)
1997
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC168645/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9292989/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.63.9.3385-3389.1997 |
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