Four Ferredoxins from Japanese Radish Leaves
| Autor: | Naoko Sakihama, S. Obata, Mikio Nishimura, Masateru Shin, K. Nagai |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Sequence analysis
Molecular Sequence Data Biophysics Biology Photosynthesis Peptide Mapping Biochemistry High-performance liquid chromatography Vegetables Amino Acid Sequence Amino Acids Molecular Biology Peptide sequence Ferredoxin chemistry.chemical_classification Sequence Homology Amino Acid Component (thermodynamics) Protein primary structure Peptide Fragments Amino acid chemistry Ferredoxins Sequence Analysis Plant Shoots |
| Zdroj: | Archives of Biochemistry and Biophysics. 316:797-802 |
| ISSN: | 0003-9861 |
| DOI: | 10.1006/abbi.1995.1106 |
| Popis: | We detected three ferredoxin components, a, b, and c, in green shoots of Japanese radish seedlings by hydrophobic HPLC analysis using a phenyl-5PW column. All components were also present in mature leaves. Component a was further separated into two components, a1 and a2, by reversed-phase HPLC after carboxymethylation. The existence of four ferredoxins in the photosynthetic tissue of a single plant species is reported here for the first time. Each individual ferredoxin component was isolated, and its primary structure was analyzed for comparison with the two leaf ferredoxins, L-Fds A and B, isolated by Wada et al. (J. Biochem. 105, 619-625 (1989)). The primary structures of components a1, a2, and b were all found in 12 possible structures of L-Fd A deducible from its microheterogeneities. This led us to conclude that L-Fd A is a mixture of three ferredoxins corresponding to components a1, a2, and b. The complete primary structure of component c was established by sequencing of the whole protein and of peptides generated by protease digestion. The N-terminal structure of component c was identical with L-Fd B up to the 11th amino acid residue, suggesting that this component is the same ferredoxin as L-Fd B. |
| Databáze: | OpenAIRE |
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