Isolation and characterization of a supramolecular complex of subunit III of the ATP-synthase from chloroplasts

Petra Fromme, Peter Gräber, Egbert J. Boekema

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In SDS gels of purified, highly active ATP-synthase from chloroplasts, CF0F1, a protein band was detected at an apparent m olecular weight of 100 kDa. This protein was isolated on a preparative SDS gel. The 100 kD a protein can be dissociated at increased tem perature or increased incubation time into an 8 kDa protein, which isidentical with the subunit III of CF0(DCCD-binding protein or proteolipid). This implies that the 100 kDa band is a stable supramolecular com plex containing at least 12 copies of subunit III. Electron micrographs reveal a diam eter of 6.3 nm and a mem brane spanning length of 6.1 nm. We assume that this supramolecular complex represents a stablenative substructure of CF0F1.

Original languageEnglish
Pages (from-to)1239-1245
Number of pages7
JournalZeitschrift fur Naturforschung - Section C Journal of Biosciences
Issue number11-12
Publication statusPublished - Dec 1 1987



  • ATP-Synthase
  • CFF
  • Chloroplasts
  • Subunit III
  • Subunits of CF

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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