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pubmed-article:7999129pubmed:abstractTextWe 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.lld:pubmed
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pubmed-article:7999129pubmed:dateRevised2003-11-14lld:pubmed
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pubmed-article:7999129pubmed:year1994lld:pubmed
pubmed-article:7999129pubmed:articleTitleHistidyl phosphorylation of P36 in rat hepatoma Fao cells in vitro and in vivo.lld:pubmed
pubmed-article:7999129pubmed:affiliationDepartment of Biochemistry, School of Pharmaceutical Sciences, Toho University, Chiba, Japan.lld:pubmed
pubmed-article:7999129pubmed:publicationTypeJournal Articlelld:pubmed