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J Bacteriol. 1968 December; 96(6): 1903-1911
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Effect of Bacterial Endotoxin and Inhibitors on Tryptophan Oxygenase Induction in Mouse Liver Slices¹

^a Department of Biology, Bryn Mawr College, Bryn Mawr, Pennsylvania 19010

ABSTRACT

Tryptophan oxygenase activity in mouse liver slices maintained in cluture medium, in Krebs-Ringer bicarbonate solution, or in homologous whole blood declined within 3 hr to about one-half the original level. Actinomycin D and puromycin accelerated the rate of decline, but endotoxin did not. Direct addition of tryptophan to the medium resulted in a higher than normal tryptophan oxygenase activity within 1 hr, and this was maintained well above that of control liver slices up to 6 hr. Triamcinolone, at a dose that doubles tryptophan oxygenase activity in vivo, had no effect on the enzyme in liver slices. Actinomycin and endotoxin did not alter the substrate induction of tryptophan oxygenase; however, puromycin did, but to a limited extent. Liver slices prepared from mice 4 hr after an injection of cortisone had a greater tryptophan oxygenase activity than those of controls. Either endotoxin or actinomycin D resulted in a more rapid decline of the enzyme when added to the slices than was observed in the controls.

² Present address: Department of Microbiology, University of Michigan School of Medicine, Ann Arbor, Mich. 48104.

¹ This study is taken from a dissertation presented to Bryn Mawr College in partial fulfillment of the requirements for the Ph.D. degree.