Abstract
Previously, a ferredoxin-type iron-sulfur protein, frx B protein, was identified in a high-salt extract of the purified thylakoid membrane of Chlamydomonas reinhardtii, a unicellular green alga. Polyclonal antibody was raised against a synthetic pentadecameric peptide with an amino acid sequence corresponding to the highly conserved region of the putative frx B proteins of 3 land plants [21]. In this report, protein(s) reacting strongly and specifically with this antibody was detected in the equivalent high-salt extract prepared from purified chloroplast of spinach and tobacco. One strong reaction polypeptide band from tobacco chloroplast was purified from SDS-polyacrylamide gel and subjected to endoproteinase lys C digestion. The resulting polypeptides were separated by reversed-phase chromatography. N-terminal sequencing of 3 purified polypeptides revealed that the protein is encoded by the 'frxB gene' identified from DNA sequence analysis.
| Original language | English |
|---|---|
| Pages (from-to) | 449-455 |
| Number of pages | 7 |
| Journal | Plant Molecular Biology |
| Volume | 15 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Sept 1990 |
| Externally published | Yes |
Keywords
- chloroplast
- frx B protein
- spinach
- tobacco
- western blot