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. 1980 Oct;66(4):605–608. doi: 10.1104/pp.66.4.605

Thioredoxin-like Activity of Thylakoid Membranes

THIOREDOXIN CATALYZING THE REDUCTIVE INACTIVATION OF GLUCOSE-6-PHOSPHATE DEHYDROGENASE OCCURS IN BOTH SOLUBLE AND MEMBRANE-BOUND FORM 1

Anthony R Ashton 1,2, Thomas Brennan 1,3, Louise E Anderson 1
PMCID: PMC440688  PMID: 16661487

Abstract

The inactivation of pea 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, however, be ascribed to the trapping of stroma since less than 0.1% of three stromal marker enzymes are found in the same thylakoid extract.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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