Abstract
The structure of ribulose-1,5-bisphosphate carboxylase (Rubisco) subunit-binding protein and its interaction with pea leaf chloroplast Rubisco were studied by electron microscopy and image analysis. Electron-microscopic evidence for the association of Rubisco subunit-binding protein, consisting of 14 subunits arranged with 72 point group symmetry, and oligomeric (L8S8) Rubisco was obtained.
Original language | English |
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Pages (from-to) | 205-209 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 289 |
Issue number | 2 |
DOIs | |
Publication status | Published - 9-Sept-1991 |
Keywords
- RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE (RUBISCO)
- RUBISCO SUBUNIT-BINDING PROTEIN
- QUATERNARY STRUCTURE
- PROTEIN-PROTEIN COMPLEX
- ELECTRON MICROSCOPY
- RIBULOSE BISPHOSPHATE CARBOXYLASE
- MOLECULAR CHAPERONES
- ESCHERICHIA-COLI
- GROE
- IDENTIFICATION
- CHLOROPLASTS
- MITOCHONDRIA
- OXYGENASE