## Abstract The model iron‐sulfur (Fe‐S) protein ferredoxin (Fd) from __Synechocystis sp__. PCC 6803 has been simultaneously produced and matured in a cell‐free production system. After 6 h of incubation at 37°C, Fd accumulated to >450 µg/mL. Essentially all was soluble, and 85% was active. Product
A ferredoxin-type iron-sulfur protein gene, frx B, is expressed in the chloroplasts of tobacco and spinach
✍ Scribed by Cheng-Hui Lin; Madeline Wu
- Publisher
- Springer
- Year
- 1990
- Tongue
- English
- Weight
- 947 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0167-4412
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✦ Synopsis
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. 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.
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