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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.
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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 | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
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Journal or Publication Title: | FEBS LETTERS | ||||
Publisher: | ELSEVIER SCIENCE BV | ||||
ISSN: | 0014-5793 | ||||
Official Date: | 1 September 2000 | ||||
Dates: |
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Volume: | 480 | ||||
Number: | 2-3 | ||||
Number of Pages: | 6 | ||||
Page Range: | pp. 271-276 | ||||
Publication Status: | Published |
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