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- W2032467523 abstract "1. Intraperitoneal injection of histones, poly l-Lys, poly l-Ala, or poly l-Tyr into adrenalectomized mice results in increases in hepatic tyrosine-α-ketoglutarate transaminase (l-tyrosine:2-oxoglutarate aminotransferase, EC 2.6.1.5) and tryptophan pyrrolase (l-tryptophan:oxygen oxidoreductase, EC 1.13.1.12) which reach peak activities in 5–6 h. Bovine plasma albumin, poly l-Leu, poly dl-Trp, poly l-Asp, poly l-Phe, and poly Gly do not have these effects at the dosages tested. At some dosages poly l-Arg increased tyrosine transaminase activities but not tryptophan pyrrolase. 2. Various basic polypeptides and histone fractions differ considerably in their ability to “induce” increases in tryptophan pyrrolase and tyrosine transaminase. These “inductions” are inhibited by puromycin and actinomycin D. 3. The half-life of hepatic tryptophan pyrrolase, induced to high levels of activity in adrenalectomized mice by injection of hydrocortisone and tryptophan, was increased from 1 to 4.3 h by injection of 2 mg poly l-Lys, and the half-life of tyrosine transaminase was increased from 3 to 6.5 h. Injected histones also increased the half-lives of these enzymes but less effectively than poly l-Lys. 4. The kinetic data indicate that the “induction” of tryptophan pyrrolase by poly l-Lys and histones results from decreased rate of enzyme degradation rather than increased rate of enzyme synthesis. On the other hand, histones and poly l-Lys appear to have a small stimulatory effect upon the rate of synthesis of tyrosine transaminase in addition to decreasing the rate of degradation of this enzyme." @default.
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- W2032467523 date "1968-05-01" @default.
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- W2032467523 title "Induction of hepatic tryptophan pyrrolase and tyrosine transaminase by histones and other polypeptides" @default.
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- W2032467523 doi "https://doi.org/10.1016/0005-2787(68)90159-7" @default.
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