Abstract
Negative staining of purified spinach dicyclohexylcarbodiimide (DCCD) sensitive ATPase revealed a population of 110 Å subunits attached by stalks to short string-like aggregates. The interpretation of these data is that 110 Å CF1 are attached by stalks to an aggregate of CF0. The CF1-CF0 complex was incorporated into phospholipid vesicles; freezefracture analysis of this preparation revealed a homogeneous population of particles spanning the lipid bilayer; these averaged 96 Å in diameter. The DCCD binding proteolipid (apparent molecular weight 7500), an integral component of CF0, was isolated from membranes by butanol extraction and was incorporated rated into phospholipid vesicles. Freeze-fracture analysis of the DCCD-binding proteolipid/vesicle preparation revealed a population of particles averaging 83 Å in diameter suggesting that the DCCD-binding proteolipid self-associates in lipid to form a stable complex. This complex may be required for proton transport across chloroplast membranes in vivo. The size difference between CF0 and DCCD-proteolipid freeze-fracture particles may be related to differences in polypeptide composition of the two complexes.
Original language | English (US) |
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Pages (from-to) | 149-157 |
Number of pages | 9 |
Journal | BBA - Biomembranes |
Volume | 642 |
Issue number | 1 |
DOIs | |
State | Published - Mar 20 1981 |
Externally published | Yes |
Keywords
- (Chloroplast)
- ATPase
- Coupling factor
- Dicyclohexylcarbodiimide
- Proteolipid
- Reconstitution
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Cell Biology