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Purification and properties of adenosine 5′-triphosphate–D-glucose 6-phosphotransferase from rat liver

1. An 870-fold purification of glucokinase from rat liver is described which involves ammonium sulphate fractionation and the use of DEAE-Sephadex, DEAE-cellulose and polyacrylamide columns. 2. The preparation is free of any interfering enzymes and has a specific activity of 8μmoles/min./mg. of prot...

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Detalles Bibliográficos
Autores principales: Parry, M. J., Walker, D. G.
Formato: Artigo
Lenguaje:Inglês
Publicado: 1966
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1264993/
https://ncbi.nlm.nih.gov/pubmed/5944237
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