Phenylalanine-induced phosphorylation and activation of rat hepatic phenylalanine hydroxylase in vivo.
نویسندگان
چکیده
منابع مشابه
In vitro activation of rat liver phenylalanine hydroxylase by phosphorylation.
Essentially pure phenylalanine hydroxylase from rat liver can be activated between 2.5- and 3.0-fold by treatment with Mg2+, ATP, protein kinase, and cyclic AMP. The activation is seen when the hydroxylase is assayed in the presence of tetrahydrobiopterin, but not in the presence of 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine. In the presence of [gamma-32P]ATP, activation is accompanied b...
متن کاملPhenylalanine-induced Phosphorylation and Activation
Rats were given intraperitoneal injections of 2 mCi of carrier-free "Pi and substances known to activate liver phenylalanine hydroxylase. After 30 min, these animals were anesthetized and their livers removed for analysis of enzyme activity, 32Pi ncorporation into immunoprecipitated phenylalanine hydroxylase and [yS2P]ATP specific activity. Following glucagon treatment, rat liver phenylalanine ...
متن کاملEffect of glucagon on hepatic phenylalanine hydroxylase in vivo.
Moderate doses of glucagon (20 micrograms/kg I.V.) are sufficient to stimulate rat hepatic phenylalanine hydroxylase in vivo. In addition, the stimulation of the tetrahydrobiopterin-dependent phenylalanine hydroxylase activity in livers of animals fed on a high-protein diet has been correlated with an elevated phosphate content. The tetrahydrobiopterin-dependent hydroxylase activity in these an...
متن کاملRelationship between the multiple forms of rat hepatic phenylalanine hydroxylase and degree of phosphorylation.
The two major forms of rat liver phenylalanine hydroxylase have been resolved by calcium phosphate chromatography and have been highly purified. These different forms of the enzyme contain dissimilar amounts of endogenous protein-bound phosphate. The hydroxylase activity of these forms, as assayed in the presence of tetrahydrobiopterin, can be differentially stimulated by treatment with Mg2+, A...
متن کاملPurification and state of activation of rat kidney phenylalanine hydroxylase.
Phenylalanine hydroxylase, the enzyme that catalyzes the irreversible hydroxylation of phenylalanine to tyrosine, was purified from rat kidney with the use of phenyl-Sepharose, DEAE-Sephacel, and gel permeation high pressure liquid chromatography. Our most highly purified fractions had a specific activity in the presence of 6-methyltetrahydropterin, of 1.5 mumol of tyrosine formed/min/mg of pro...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1992
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)48367-6