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Plant Physiology 90:977-981 (1989)
© 1989 American Society of Plant Biologists

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Metabolism and Enzymology

Partial Purification and Characterization of Three Flavonol-Specific Sulfotransferases from Flaveria chloraefolia1

Luc Varin and Ragai K. Ibrahim

Plant Biochemistry Laboratory, Department of Biology, Concordia University, Montreal, Quebec, Canada H3G 1M8

Three distinct flavonol-specific sulfotransferases were partially purified from the shoot tips of Flaveria chloraefolia A. Gray by fractional precipitation with ammonium sulfate, followed by gel filtration on Sephacryl S-200, 3'-phosphoadenosine 5-phosphate-Agarose affinity chromatography and chromatofocusing on Mono P. These enzymes exhibited expressed specificity for positions 3 of various flavonol acceptors and of 3' and 4' of flavonol 3-sulfate. The three sulfotransferases had similar molecular weights (35,000), exhibited no requirement for divalent cations and were not inhibited by SH group reagents. Their Km values for both the sulfate donor and the flavonol acceptors were of the same order of magnitude (ca. 0.2-0.4 micromolar). Except for the 3-sulfotransferase, which exhibited two optima at pH 6.5 and 8.5, the 3' and the 4'-sulfotransferases had a pH optimum of 7.5. The three enzymes could be resolved only by chromatofocusing and were eluted at pH 5.4, pH 6.0, and pH 5.1 for the 3-, 3'- and 4'-sulfotransferases, respectively. The substrate specificity of these three enzymes is discussed in relation to the biosynthesis of polysulfated flavonols in F. chloraefolia.

1 This work was supported by the Natural Sciences and Engineering Research Council of Canada and the Department of Higher Education, Government of Quebec. L. V. was the recipient of an NSERC post-graduate scholarship and a Concordia University Fellowship. Presented in part at the 14th International Conference of Groupe Polyphenols, St. Catherines, Ontario, August 1988.




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