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...

Descripció completa

Dades bibliogràfiques

Publicat a:	J Bacteriol
Autors principals:	Friedrich, B, Friedrich, C G, Schlegel, H G
Format:	Artigo
Idioma:	Inglês
Publicat:	American Society for Microbiology (ASM) 1976
Matèries:	Research Article
Accés en línia:	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
Etiquetes:	Afegir etiqueta Sense etiquetes, Sigues el primer a etiquetar aquest registre!