Thioredoxin-like Activity of Thylakoid Membranes
- 1 October 1980
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 66 (4), 605-608
- https://doi.org/10.1104/pp.66.4.605
Abstract
The inactivation of pea [Pisum sativum] leaf chloroplast glucose-6-phosphate dehydrogenase by dithiothreitol can be catalyzed by thioredoxin-like molecules that are present in chloroplasts. This thioredoxin activity occurs predominantly as a soluble species, but washed thylakoid membranes also exhibit some thioredoxin-like activity. The membrane-associated thioredoxin can be extracted by treatment with the detergent Triton X-100. The solubilized thioredoxin appears to have a molecular size similar to that of the soluble thioredoxin which catalyzes the same reaction. The thylakoid-bound activity constitutes only about 5% of the total chloroplast thioredoxin activity. The thioredoxin occurring in the membrane fraction cannot be ascribed to trapping of stroma since less than 0.1% of 3 stromal marker enzymes are found in the same thylakoid extract.Keywords
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