Partial Purification and Characterization of the Maize Mitochondrial Pyruvate Dehydrogenase Complex
The pyruvate dehydrogenase complex was partially purified and characterized from etiolated maize (Zea mays L.) shoot mitochondria. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed proteins of 40, 43, 52 to 53, and 62 to 63 kD. Immunoblot analyses identified these proteins...
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| Vydáno v: | Plant Physiol |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Oxford University Press
1998
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC35052/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9536062/ https://ncbi.nlm.nih.govhttps://doi.org/10.1104/pp.116.4.1443 |
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