Results 1 to 10 of about 16,690 (208)
RNAi-induced silencing of embryonic tryptophan oxygenase in the Pyralid moth, Plodia interpunctella [PDF]
Journal of Insect Science, 2004 Gene silencing through the introduction of double-stranded RNA (RNA interference, RNAi) provides a powerful tool for the elucidation of gene function in many systems, including those where genomics and proteomics are incomplete.
Jeffrey A. Fabrick +2 more
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Regulatory Properties of Hepatic Tryptophan Oxygenase
Journal of Biological Chemistry, 1972 Abstract The kinetic properties of highly purified hepatic l-tryptophan oxygenase have been studied at different hydrogen ion concentrations in the absence and presence of dl-α-methyltryptophan and 3-hydroxyanthranilic acid. At pH 8.0 plots of velocity versus l-tryptophan concentrations indicate classical hyperbolic Michaelis-Menten kinetics, whereas ...
G, Schutz, E, Chow, P, Feigelson
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The Prematurely Evoked Synthesis of Liver Tryptophan Oxygenase [PDF]
Proceedings of the National Academy of Sciences, 1971 Livers of normal rats are devoid of catalytically or immunochemically reactive tryptophan oxygenase (EC 1.13.1.12) up to the 10th postnatal day; the enzyme reaches adult concentrations on about the twentieth day. Premature tryptophan oxygenase synthesis can be evoked in 4-day-old rats: if an injection of glucocorticoid is followed, a day later, by an ...
O, Greengard, H K, Dewey
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Inhibition of tryptophan oxygenase in rat liver by steroid hormones [PDF]
Biochemical Journal, 1970 Pregnant women and normal humans treated with estrogens show evidence of increased conversion of L-tryptophan into nicotinic acid ribonucleotide. Increased activity of liver tryptophan oxygenase caused by the action of estrogens or elevated corticosteroid concentration is thought to be the cause. Progesterone caused a decrease in tryptophan oxygenase
I P, Braidman, D P, Rose
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DEGRADATION OF TRYPTOPHAN OXYGENASE IN VIVO AND IN VITRO. [PDF]
, 1972 The loss of tryptophan oxygenase from rat livers after induction by hydrocortisone treatment was studied in living rats, isolated perfused livers, liver slices and cell-free preparations of these livers. Measurements of the enzyme by its activity and as an antigen were parallel except for apparently non-specific inactivations in some incubations of ...
Li, J B, Knox, W E
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Immunological Quantitation of Hepatic Tryptophan Oxygenase in Endotoxin-Poisoned Mice [PDF]
Infection and Immunity, 1973 An apparent inhibition of induction of mouse hepatic tryptophan oxygenase by endotoxin has been reported previously, as evidenced by low catalytic activity. This could be due either to decreased tryptophan oxygenase levels or to inactivation of existing enzyme molecules.
D F, Rippe, L J, Berry
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Inactivation of Tryptophan Oxygenase in Vivo and in Vitro
Journal of Biological Chemistry, 1972 Abstract The loss of tryptophan oxygenase from rat livers after induction by hydrocortisone treatment was studied in living rats, isolated perfused livers, liver slices and cell-free preparations of these livers. Measurements of the enzyme by its activity and as an antigen were parallel except for apparently nonspecific inactivations in some ...
J B, Li, W E, Knox
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Titration of Tryptophan Oxygenase Antigen by Immunoinhibition [PDF]
Journal of Biological Chemistry, 1972 J B, Li, W E, Knox
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Tryptophan Oxygenase of Pseudomonas acidovorans
Journal of Biological Chemistry, 1969 W N Poillon +3 more
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Journal of Biological Chemistry, 1967 1. The substrate, tryptophan, forms spectrophotometrically detectable enzyme-substrate complexes with tryptophan oxygenase (EC 1.13.1.12)—commonly known as tryptophan pyrrolase—when the iron atom of the heme prosthetic group is either divalent, trivalent, or combined with carbon monoxide. 2.
H, Maeno, P, Feigelson
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