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...

Ausführliche Beschreibung

Bibliographische Detailangaben

Veröffentlicht in:	Journal of bacteriology Jg. 183; H. 19; S. 5491
Hauptverfasser:	Afshar, S, Johnson, E, de Vries, S, Schröder, I
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	United States 01.10.2001
Schlagworte:	Enzyme Stability Hydrogen-Ion Concentration Kinetics Molecular Weight Molybdoferredoxin Nitrate Reductase Nitrate Reductases - chemistry Nitrate Reductases - isolation & purification Nitrate Reductases - metabolism Protein Subunits Temperature Thermoproteaceae - enzymology
ISSN:	0021-9193
Online-Zugang:	Weitere Angaben
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!