Pyrrolooxygenases: a new type of oxidases.
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Biomedical subjects
Publications and source records attributed to R B Frydman.
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Sucrose and sucrose 6-phosphate synthetase were isolated from potato tubers, partially purified and their properties studied. The sucrose synthetase showed optimum activity at 45 degrees and was inhibited competitively by ADP and some phenolic glucosides. The Ki's for these inhibitors were determined. Mg(2+) was found to activate this enzyme. Activity toward UDP-glucose or ADP-glucose formation was measured. The optimum conditions for sucrose and UDP-glucose formation were found to differ. The specificity for the glucosyl donor and acceptor were determined.The optimum conditions for sucrose 6-phosphate synthetase activity were studied. This enzyme was not inhibited by either ADP or phenolic glucosides; UDP-glucose was the only glucosyl donor for sucrose 6-phosphate formation.
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When potato sprouts or potato tuber slices were incubated with 0.1 m glucose 1-phosphate, a soluble amylopectin-like polysaccharide was excreted to the medium. This polysaccharide was found to be a very good primer for phosphorylase and a poor one for starch synthetase. Beside the formation of this extracellular polysaccharide, a more branched intracellular polysaccharide could be isolated. This polysaccharide was an excellent primer for starch synthetase. Fructose 6-phosphate, glucose 6-phosphate, fructose 1,6-diphosphate, glucose or sucrose could not substitute for glucose 1-phosphate. 2,4-Dinitrophenol or nitrogen did not affect the excretion of the polysaccharide. Some properties of these 2 polysaccharides are described.
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