Linked Life Data

690116

Source:http://linkedlifedata.com/resource/pubmed/id/690116

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1978-11-29
pubmed:abstractText
Phenylalanine hydroxylase activities in extracts of livers from rats pretreated with glucagon are higher than in controls. This time-dependent 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-dimethyltetrahydropterin. A maximum 4-fold stimulation of hydroxylase activity was correlated with a conversion of the multiple forms of the enzyme to a single form. This form is characterized by an increased extent of phosphorylation compared to the unactivated enzyme. Incorporation of radioactive inorganic phosphate into phenylalanine hydroxylase following administration of glucagon was determined after specific immunoprecipitation of the enzyme from partially purified preparations. Sodium dodecyl sulfate disc gel electrophoresis showed that stimulation of enzyme activity is accompanied by incorporation of 32Pi into the protein to the extent of 0.7 mol/mol of hydroxylase subunit. These results demonstrate the phosphorylation of hepatic phenylalanine hydroxylase in vivo and strongly support the idea that the activity of this enzyme can be hormonally regulated through a phosphorylation mechanism.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6657-9
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Glucagon stimulation of rat hepatic phenylalanine hydroxylase through phosphorylation in vivo.
pubmed:publicationType
Journal Article