Results 201 to 210 of about 39,051 (241)
Some of the next articles are maybe not open access.
Molecular Biology of Phenylalanine Hydroxylase
Journal of Inherited Metabolic Disease, 1986Phenylalanine hydroxylase (PH; EC 1.14.16.1) is a complex enzyme with three substrates and three activators. Little is known about the structural features which are necessary for the function of this enzyme; only the phosphorylation site is known (Wretburn et al., 1980).
R. G. F. Cotton +7 more
openaire +1 more source
Phenylalanine hydroxylase: metabolic aspects
Biochemical Society Transactions, 1985Phenylalanine hydroxylase [L-phenylalanine,tetrahydropteridine :oxygen oxidoreductase (4-hydroxylating); EC 1.14.16.11 catalyses the first reaction in the irreversible catabolism of the essential amino acid phenylalanine. Studies of the isolated enzyme and of phenylalanine metabolism in viuo and in oitro support the view that the hydroxylase plays the ...
C I, Pogson, M A, Santana, M J, Fisher
openaire +2 more sources
Treatment of phenylalanine hydroxylase deficiency
Acta Paediatrica, 1994In phenylalanine hydroxylase deficiency detected by screening treatment in early life, both age at start of treatment and phenylalanine control during treatment are the major determinants of eventual psychological status. The influence of phenylalanine control declines with age but executive performance is influenced by hyperphenylalaninaemia at all ...
openaire +2 more sources
Phenylalanine hydroxylase activity in mammalian cells
Journal of Cellular Physiology, 1969AbstractSurvey of twelve mouse tissues revealed the presence of appreciable phenylalanine hydroxylase activity in the pancreas and kidney as well as the liver but in no other of the tissues tested. Single cell suspensions of mouse liver were prepared by use of tetraphenylboron.
A, Tourian, J, Goddard, T T, Puck
openaire +2 more sources
Mutagenesis of the regulatory domain of phenylalanine hydroxylase
Proceedings of the National Academy of Sciences, 2001The regulatory domain of phenylalanine hydroxylase (PAH, EC 1.14.16.1 ) consists of more than 100 amino acids at the N terminus, the removal of which significantly activates the enzyme. To study the regulatory properties controlled by the N terminus, a series of truncations and site-specific mutations were made ...
G A, Wang, P, Gu, S, Kaufman
openaire +2 more sources
Phenylalanine hydroxylase in dilute lethal mice
Biochimica et Biophysica Acta (BBA) - General Subjects, 1973Abstract The steady-state specific activity of hepatic phenylalanine hydroxylase in the 19–20-day-old dilute lethal mouse d 1 / d 1 is 2-fold higher than in its wild-type control D / D . The apparent K m values for phenylalanine and tetrahyfropteridine are identical for mutant and control enzymes.
Treiman, D M, Tourian, A
openaire +2 more sources
Hepatic Phenylalanine Hydroxylase and PKU
1975The conversion of phenylalanine to tyrosine in mammalian tissues is catalyzed by a complex enzyme system composed of several essential enzymes and cofactors. All of these components have been assayed in liver biopsy samples from patients with the classic form of PKU.
openaire +2 more sources
Diagnosis of Phenylalanine Hydroxylase Deficiency (Phenylketonuria)
Archives of Pediatrics & Adolescent Medicine, 1982Needle liver biopsies were carried out on patients with phenylketonuria (PKU) to establish a diagnosis either of partial or complete phenylalanine hydroxylase (PH) deficiency. Ten phenylketonuric patients and two parents were studied. Nine of the ten patients had completed a three-day oral phenylalanine challenge.
H K, Berry +3 more
openaire +2 more sources
Inactivation of purified phenylalanine hydroxylase by dithiothreitol
Biochemical and Biophysical Research Communications, 1992Purified rat liver phenylalanine hydroxylase is inactivated in vitro by ascorbate and thiol compounds, dithiothreitol being the most effective inhibitor, with a second order rate constant for the inactivation of 0.066 +/- 0.002 mM-1.min-1 at 20 degrees C and pH 7.2.
A, Martínez +3 more
openaire +2 more sources
A simple radioisotope assay for phenylalanine hydroxylase
Analytical Biochemistry, 1967Abstract An isotopic assay for phenylalanine hydroxylase activity has been devised. The assay involves incubation of the enzyme with p -tritio- l -phenylalanine followed by the addition of N -iodosuccinimide to iodinate the tyrosine produced. The tritium released by this combination appears as tritiated water and is proportional to the amount of ...
G, Guroff, A, Abramowitz
openaire +2 more sources