Purification and characterization of the inhibitory subunit (delta) of the ATP synthase from Micrococcus luteus
FEBS letters. Bd. 356. H. 2-3. Amsterdam u.a.: Elsevier 1994 S. 226 - 228
Erscheinungsjahr: 1994
ISBN/ISSN: 0014-5793
Publikationstyp: Zeitschriftenaufsatz
Sprache: Englisch
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Inhaltszusammenfassung
Subunit delta was isolated from the ATP-synthase from Micrococcus luteus strain (ATCC 4698). delta, in the case of M. luteus F0F1-ATPase, acts as an inhibitor of ATP hydrolysis and thus resembles subunits in E. coli and chloroplast ATP-synthase. After treatment with 1.5 M LiCl the ATP-synthase dissociated, and subsequently subunit delta (27 kDa) was purified by hydrophobic interaction chromatography. Inhibition of ATP-synthase lacking delta by addition of delta showed non-competitive kinetics...Subunit delta was isolated from the ATP-synthase from Micrococcus luteus strain (ATCC 4698). delta, in the case of M. luteus F0F1-ATPase, acts as an inhibitor of ATP hydrolysis and thus resembles subunits in E. coli and chloroplast ATP-synthase. After treatment with 1.5 M LiCl the ATP-synthase dissociated, and subsequently subunit delta (27 kDa) was purified by hydrophobic interaction chromatography. Inhibition of ATP-synthase lacking delta by addition of delta showed non-competitive kinetics with a Ki of approximately 5.9 nM. Subunit epsilon from chloroplast F1, which corresponds functionally to the M. luteus F0F1-delta, and chloroplast delta were tested for ATPase inhibitory activity by addition to the partially delta-depleted ATP-synthase from M. luteus. CF1-epsilon inhibited M. luteus ATP-synthase up to 80%, whereas CF1-delta did not show any influence.» weiterlesen» einklappen
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Klassifikation
DFG Fachgebiet:
Grundlagen der Biologie und Medizin
DDC Sachgruppe:
Biowissenschaften, Biologie