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Variation in Glyoxylate Bypass Inducibility among Strains of Tetrahymena pyriformis
Author(s) -
KEMPER DAVID L.,
THOMPSON SIOE HOEY,
PARSONS JOHN A.
Publication year - 1973
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1973.tb00928.x
Subject(s) - isocitrate lyase , glyoxylate cycle , malate synthase , tetrahymena pyriformis , isocitrate dehydrogenase , enzyme , biochemistry , biology , idh1 , malate dehydrogenase , chemistry , tetrahymena , gene , mutation
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.