Linked Life Data

6679751

Source:http://linkedlifedata.com/resource/pubmed/id/6679751

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1984-11-2
pubmed:abstractText
Phenylalanine hydroxylase from fresh human liver was purified to homogeneity with a 60% yield by a three steps procedure involving hydrophobic chromatography on Phenyl-Sepharose, ion exchange chromatography on DEAE-Cellulose and High Performance gel permeation chromatography. The purified native enzyme had an estimated molecular weight of 165,000. It gave a single band on Sodium Dodecylsulfate polyacrylamide gel electrophoresis under an estimated molecular weight of 55,000. Neither the purified human enzyme, nor that present in a liver extract could be activated under phosphorylating conditions. Moreover, the purified human liver phenylalanine hydroxylase was found to be devoid of protein-bound phosphate and no phosphate could be incorporated from [32P]-ATP in the presence of cyclic-AMP - dependent protein kinase. These data suggest that phenylalanine hydroxylase from human liver, unlike that of rat liver, might not be a phosphoprotein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
727-37
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Phenylalanine hydroxylase. Evidence that the enzyme from human liver might not be a phosphoprotein.
pubmed:publicationType
Journal Article