PURIFICATION AND CHARACTERIZATION OF THE INHIBITORY SUBUNIT-(DELTA) OF THE ATP-SYNTHASE FROM MICROCOCCUS-LUTEUS
Autor(en): | GRUBER, G ENGELBRECHT, S JUNGE, W DOSE, K NAWROTH, T |
Stichwörter: | ADENOSINE-TRIPHOSPHATASE; ATP-SYNTHASE; ATPASES; Biochemistry & Molecular Biology; Biophysics; Cell Biology; CF1; COMPLEX; DELTA SUBUNIT; ENZYMES; EPSILON SUBUNIT; EPSILON-SUBUNIT; ESCHERICHIA-COLI; INHIBITOR PROTEIN; MICROCOCCUS LUTEUS; PHOTOPHOSPHORYLATION; RECONSTITUTION | Erscheinungsdatum: | 1994 | Herausgeber: | ELSEVIER SCIENCE BV | Journal: | FEBS LETTERS | Volumen: | 356 | Ausgabe: | 2-3 | Startseite: | 226 | Seitenende: | 228 | Zusammenfassung: | 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-competitve kinetics with a K-i of similar to 5.9 nM. Subunit epsilon from chloroplast F-1, 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. |
ISSN: | 00145793 | DOI: | 10.1016/0014-5793(94)01271-7 |
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geprüft am 23.05.2024