Linked Life Data

6481178

Source:http://linkedlifedata.com/resource/pubmed/id/6481178

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1984-11-9
pubmed:abstractText
Polyamine-dependent protein kinase in cytosol of pig epidermal cells was extracted. The fraction containing this enzyme exhibited multiple polypeptide bands on polyacrylamide gel electrophoresis, including 4 major polypeptide bands and several minor polypeptide bands. A 80 kilodalton (KD) polypeptide, one of the minor polypeptide bands, was phosphorylated by polyamine-dependent protein kinase. Authentic ornithine decarboxylase (ODC) exogenously added was separated into 2 subunits (80 KD and 40 KD) on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and a 80 KD polypeptide was also phosphorylated by polyamine-dependent protein kinase. A 80 KD polypeptide of ODC comigrated with the polypeptide of cytosol which was phosphorylated by polyamine-dependent protein kinase. Kinetic study revealed that the ODC activity decreased as ODC was phosphorylated. Therefore, ODC activity was inhibited by epidermal polyamine-dependent protein kinase-mediated phosphorylation. The overall results indicate that the rapid turnover of ODC might be regulated by a phosphorylation-dephosphorylation reaction without new protein synthesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-202X
pubmed:author
pubmed:issnType
Print
pubmed:volume
83
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
257-60
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Ornithine decarboxylase activity is inhibited by epidermal polyamine-dependent protein kinase-mediated phosphorylation.
pubmed:publicationType
Journal Article