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Purification and characterization of a dUTPase from Acholeplasma laidlawii B-PG9.

dUTP was purified 120-fold from extracts of Acholeplasma laidlawii B-PG9 by Blue-Sepharose, Phenyl-Sepharose, hydroxyapatite, and DEAE-Sephacel chromatography techniques. The only substrate for the enzyme was dUTP with an apparent Km of 4.5 microM. The only reaction products were dUMP and PPi. The d...

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Autors principals: Williams, M V, Pollack, J D
Format: Artigo
Idioma:Inglês
Publicat: 1984
Matèries:
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC215625/
https://ncbi.nlm.nih.gov/pubmed/6145699
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