Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-1-17
pubmed:abstractText
We have previously shown that a membrane-associated P36 from rat liver was in vitro phosphorylated at His residue(s) with a phosphoric amide bond (FEBS Lett., 319:75-79, 1993), and the activity was solubilized and partially purified (J. Biol. Chem., 269:9030-9037, 1994). The present study demonstrates that the P36 histidyl phosphorylation occurs in rat hepatoma cells under normal conditions. Phosphorylation and dephosphorylation of histidine as well as those of serine, threonine and tyrosine residues may also play an important role in animal cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
205
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
899-904
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Histidyl phosphorylation of P36 in rat hepatoma Fao cells in vitro and in vivo.
pubmed:affiliation
Department of Biochemistry, School of Pharmaceutical Sciences, Toho University, Chiba, Japan.
pubmed:publicationType
Journal Article