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Variation in Glyoxylate Bypass Inducibility among Strains of Tetrahymena pyriformis
Authors:DAVID L KEMPER  SIOE HOEY THOMPSON  JOHN A PARSONS
Institution:Gilford Instrument Laboratory, Oberlin, Ohio 44074;Department of Biochemistry, University of Iowa, Iowa City, Iowa 52240;Department of Biology, California State University, San Diego, California 92115
Abstract:SYNOPSIS. Seven strains of Tetrahymena pyriformis were assayed for log phase activity of the glyoxylate bypass enzymes isocitrate lyase and malate synthase. In strains 6I, 6II, 6III, and W, isocitrate lyase was induced; in HS, neither enzyme was induced by acetate. During growth in glucose- or acetate-containing media, strains 6III and GL had 2 periods of increased glyoxylate bypass and isocitrate dehydrogenase enzyme activities. Enzyme activities reached a maximum at the end of log phase, declined until the middle of stationary phase, and then increased again to a maximum near the end of stationary phase.
Keywords:Tetrahymena pyriformis            glyoxylate bypass induction  strain variation  isocitrate lyase  malate synthase  isocitrate dehydrogenase
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