Developmental biology of hepatic phenylalanine hydroxylase activity in foetal and neonatal rats synchronized as to conception

1972 ◽  
Vol 279 (3) ◽  
pp. 484-490 ◽  
Author(s):  
Ara Tourian ◽  
David M. Treiman ◽  
Joan S. Carr
Keyword(s):  
Developmental Biology ◽  
Phenylalanine Hydroxylase ◽  
Neonatal Rats ◽  
Hydroxylase Activity

Development of phenylalanine hydroxylase activity in guinea pig liver

1972 ◽  
Vol 261 (2) ◽  
pp. 315-320 ◽  
Author(s):  
Helen K. Berry ◽  
Roberta Cripps ◽  
Kay Nicholls ◽  
David McCandless ◽  
Calvin Harper
Keyword(s):  
Guinea Pig ◽  
Phenylalanine Hydroxylase ◽  
Hydroxylase Activity ◽  
Pig Liver ◽  
Guinea Pig Liver

Comparison of Different Methods for the Determination of Phenylalanine Hydroxylase Activity in Rat Liver and Euglena gracilis

1984 ◽  
Vol 39 (7-8) ◽  
pp. 728-733 ◽  
Author(s):  
Rita M. Fink ◽  
Erich F. Elstner
Keyword(s):  
Rat Liver ◽  
Euglena Gracilis ◽  
Phenylalanine Hydroxylase ◽  
Hplc Method ◽  
Enzymic Activity ◽  
Hydroxylase Activity ◽  
Product Separation ◽  
Tyrosine Concentration ◽  
Layer Chromatography

Abstract Three different methods for the determination of phenylalanine hydroxylase activity have been compared: a) Differential photometric assay of the increase in tyrosine concentration in the presence of phenylalanine; b) Product separation by thin layer chromatography and scintillation counting of the [14C]tyrosine formed;c) HPLC separation and spectrofluorometric quantification of derivatized amino acids. A comparison of the activities of phenylalanine hydroxylase in rat liver and Euglena gracilis clearly showed that only rat liver contains this enzymic activity as shown by methods b) and c) although pseudo-activity of Euglena gracilis preparations was found during the spectrophotometric test a). The HPLC method proved to be the fastest, most reliable and convenient method for direct tyrosine determination and thus for measuring phenylalanine hydroxylase activity.

scholarly journals Metabolism of phenylalanine in mice homozygous for the gene ‘dilute lethal’

1970 ◽  
Vol 119 (5) ◽  
pp. 895-903 ◽  
Author(s):  
L. I. Woolf ◽  
A. Jakubovic ◽  
F. Woolf ◽  
P. Bory
Keyword(s):  
Natural History ◽  
Phenylalanine Hydroxylase ◽  
Disease Process ◽  
Particulate Fraction ◽  
Hydroxylase Activity ◽  
Phenylpyruvic Acid ◽  
History Of

Mice homozygous for dl have been suggested as models for phenylketonuria. We found: (1) the concentration of phenylalanine in the blood was normal at all ages examined; (2) phenylalanine hydroxylase activity in the liver in vitro equalled that in unaffected littermates; (3) the apparent Km values for phenylalanine and cofactor respectively in dl/dl mice were the same as in their normal littermates; (4) inhibition of the overall reaction by the particulate fraction, excess of substrate, excess of cofactor or phenylpyruvic acid showed no difference between dl/dl mice and their unaffected littermates; (5) phenylalanine injected in vivo had equal, small, effects on phenylalanine hydroxylase activity of the liver measured in vitro in the two groups of mice. An explanation of the findings of other workers, based on the natural history of the disease process, is tentatively put forward.

Phenylalanine hydroxylase activity in mammalian cells

1969 ◽  
Vol 73 (2) ◽  
pp. 159-170 ◽  
Author(s):  
Ara Tourian ◽  
Judy Goddard ◽  
Theodore T. Puck
Keyword(s):  
Mammalian Cells ◽  
Phenylalanine Hydroxylase ◽  
Hydroxylase Activity

Biopterin metabolism and phenylalanine hydroxylase activity during early liver regeneration

1982 ◽  
Vol 106 (3) ◽  
pp. 786-793 ◽  
Author(s):  
Jean-Louis Dhondt ◽  
Gregory Kapatos ◽  
Michael Parniak ◽  
Harvey Wilgus ◽  
Seymour Kaufman
Keyword(s):  
Liver Regeneration ◽  
Phenylalanine Hydroxylase ◽  
Hydroxylase Activity
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