Phosphoinositides are not phosphorylated by the very active tyrosine protein kinase from the murine lymphoma LSTRA

Sigmund Fischer, Remi Fagard, P. Comoglio, G. Gacon

Research output: Contribution to journalArticle

Abstract

We studied the ability to phosphorylate phosphoinositides by 3 different subcellular preparations, and immunopurified tyrosine protein kinase (TPK) from two murine lymphoma cell lines induced by the Moloney murine leukemia virus : LSTRA with a very active TPK and MBL2 without significant TPK activity. We could not find any difference in the phosphorylation of phosphoinositides by these preparations. The TPK purified with two antibodies which phosphorylate actively tyrosine on exogenous substrate were unable to phosphorylate phosphoinositides.

Original languageEnglish
Pages (from-to)481-489
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume132
Issue number2
DOIs
Publication statusPublished - Oct 30 1985

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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