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Plant Physiology 58:320-323 (1976)
© 1976 American Society of Plant Biologists

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Articles

Possible Interference by an Acid-stable Enzyme during the Extraction of Nucleoside Di- and Triphosphates from Higher Plant Tissues

Hiroshi Ikuma and Richard M. Tetley1

a Department of Cellular and Molecular Biology, Division of Biological Sciences, University of Michigan, Ann Arbor, Michigan 48109

Acid extracts from tissues of two solanaceous plants were found to contain a heat-labile, nondialyzable factor which hydrolyzes nucleoside di- and triphosphates to nucleoside monophosphates. This acid-resistant factor shows optimal ATP-hydrolyzing activity at pH 5, whereas practically no activity was detected below pH 3 and above pH 9. It does not hydrolyze sugar phosphates, nucleoside monophosphates, uridine diphosphoglucose, and phosphoenolpyruvate. In order to estimate quantitatively the amount of nucleoside di- and triphosphates in a plant extract, care must be taken to circumvent possible interference by this factor. This is achieved by carefully maintaining the extract below pH 3.


1 Present address: Department of Biology, University of Oregon, Eugene, Oregon 97403.




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S. A. Ruuska, T. J. Andrews, M. R. Badger, G. D. Price, and S. von Caemmerer
The Role of Chloroplast Electron Transport and Metabolites in Modulating Rubisco Activity in Tobacco. Insights from Transgenic Plants with Reduced Amounts of Cytochrome b/f Complex or Glyceraldehyde 3-Phosphate Dehydrogenase
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Copyright © 1976 by the American Society of Plant Biologists