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A peroxidase homologue and novel plastocyanin located by proteomics to the Arabidopsis chloroplast thylakoid lumen
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UNSPECIFIED (2000) A peroxidase homologue and novel plastocyanin located by proteomics to the Arabidopsis chloroplast thylakoid lumen. FEBS LETTERS, 480 (2-3). pp. 271-276. ISSN 0014-5793
Full text not available from this repository.Abstract
A study by two-dimensional electrophoresis showed that the soluble, lumenal fraction of Arabidopsis thaliana thylakoids can be resolved into 300 protein spots. After subtraction of low-intensity spots and accounting for low-level stromal contamination, the number of more abundant, lumenal proteins was estimated to be between 30 and 60. Two of these proteins have been identified: a novel plastocyanin that also was the predominant component of the total plastocyanin pool, and a putative ascorbate peroxidase. Import studies shamed that these proteins are routed to the thylakoid lumen by the Sec- and delta pH-dependent translocation pathways, respectively, In addition, novel isoforms of PsbO and PsbQ were identified, (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
| Journal or Publication Title: | FEBS LETTERS |
| Publisher: | ELSEVIER SCIENCE BV |
| ISSN: | 0014-5793 |
| Date: | 1 September 2000 |
| Volume: | 480 |
| Number: | 2-3 |
| Number of Pages: | 6 |
| Page Range: | pp. 271-276 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/13025 |
Data sourced from Thomson Reuters' Web of Knowledge
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