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Properties of a Thermostable Nitrate Reductase from the Hyperthermophilic Archaeon Pyrobaculum aerophilum

The nitrate reductase of the hyperthermophilic archaeon Pyrobaculum aerophilum was purified 137-fold from the cytoplasmic membrane. Based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, the enzyme complex consists of three subunits with apparent molecular weights of 130,000, 5...

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Autori principali: Afshar, Sepideh, Johnson, Eric, de Vries, Simon, Schröder, Imke
Natura: Artigo
Lingua:Inglês
Pubblicazione: American Society for Microbiology 2001
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC95438/
https://ncbi.nlm.nih.gov/pubmed/11544209
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JB.183.19.5491-5495.2001
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