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.
|Number of pages||7|
|Journal||Zeitschrift fur Naturforschung - Section C Journal of Biosciences|
|Publication status||Published - Dec 1 1987|
- Subunit III
- Subunits of CF
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)