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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| Vydáno v: | J Bacteriol |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1984
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC215625/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6145699/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.159.1.278-282.1984 |
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