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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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Autors principals: Friedrich, B, Friedrich, C G, Schlegel, H G
Format: Artigo
Idioma:Inglês
Publicat: 1976
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC233205/
https://ncbi.nlm.nih.gov/pubmed/1262315
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