Purification and properties of chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from Alcaligenes eutrophus.
Chorismate mutase and prephenate dehydratase from Alcaligenes autophus H16 were purified 470-fold with a yield of 24%. During the course of purification, including chromatography on diethylaminoethyl (DEAE)-cellulose, phenylalanine-substituted Sepharose, Sephadex G-200 and hydrogyapatite, both enzym...
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| Publicado no: | J Bacteriol |
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| Principais autores: | , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
American Society for Microbiology (ASM)
1976
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC233205/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1262315/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.126.2.712-722.1976 |
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