Subject(s)
Phosphorylases , Plants/enzymology , Starch/biosynthesis , Amylases , Chromatography, Ion Exchange , Dialysis , Drug Stability , Electrophoresis, Polyacrylamide Gel , Glucosephosphates , Guanidines , Hydrogen-Ion Concentration , Macromolecular Substances , Nucleoside Diphosphate Sugars , Phosphorylases/antagonists & inhibitors , Phosphorylases/metabolism , Phosphorylases/physiology , Plants/metabolism , Polysaccharides , Pyridoxal Phosphate , Sulfhydryl Reagents , Temperature , Time Factors , Urea , VegetablesSubject(s)
Glucosyltransferases/metabolism , Plants/enzymology , Polysaccharides/biosynthesis , Starch/biosynthesis , Cell-Free System , Chemical Precipitation , Drug Stability , Electrophoresis , Glucosyltransferases/analysis , Glucosyltransferases/antagonists & inhibitors , Plants/metabolism , Plants, Edible/enzymology , Quaternary Ammonium Compounds , Sulfates , Temperature , Time FactorsABSTRACT
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.
