E. Pavlasová

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Escherichia coli accumulates thiomethyl-/3-D-galactoside against a concentration gradient under anaerobic conditions. The accumulation was abolished by carbonylcyanide m-chlorophenylhydrazone, tetrachlorosalicylanilide, 2,4 dinitrophenol, and other uncouplers of oxidative phosphorylation even though oxidative phosphorylation would not be expected to occur(More)
During a simultaneous induction of three enzymes which are subject to catabolite repression (β-galactosidase, tryptophanase and amylomaltase, or β-galactosidase, tryptophanase and D-serine deaminase) in a batch culture, the rates of synthesis of β-galactosidase and tryptophanase decreases, while the rates of synthesis of amylomaltase and D-serine deaminase(More)
When inducing simultaneously β-galactosidase and tryptophanase in a batch culture either the synthesis of tryptophanase or of both enzymes is decreased due to an insufficient cAMP concentration. The addition of this nucleotide can overcome this decrease. In a continuous culture both enzymes are synthesized at the maximum rate, as the amount of cAMP produced(More)
Enzyme synthesis of tryptophan from indole, pyruvate and ammonium salts was studied usingEscherichia coli cells exhibiting a significant tryptophanase activity. In addition to the effect of cultivation medium composition and cultivation conditions, factors affecting the course of the conversion were investigated. Production of 32.4 g/L ofl-tryptophan was(More)
Escherichia coli accumulates thiomethyl-beta-d-galactoside against a concentration gradient under anaerobic conditions. The accumulation was abolished by carbonylcyanide m-chlorophenylhydrazone, tetrachlorosalicylanilide, 2,4 dinitrophenol, and other uncouplers of oxidative phosphorylation even though oxidative phosphorylation would not be expected to occur(More)
Enzyme activity of the hyperproducing mutants isolated from a chemostat decreases by passaging under nonselective conditions to about one half of the original value, and then remains stable. High activity can be quickly restored by transfer to chemostat selective conditions. The elaborated storage method prevents the decrease of enzyme activity after 2–3(More)