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

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 MBL 2 without significant TPK activi...

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Published inBiochemical and biophysical research communications Vol. 132; no. 2; pp. 481 - 489
Main Authors Fischer, Sigmund, Fagard, Remi, Comoglio, P., Gacon, G.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 30.10.1985
Subjects
Animals
Cell Fractionation
Cell Line
Liposomes
Lymphoma - enzymology
Mice
Mice, Inbred BALB C
Mice, Inbred C57BL
Moloney murine leukemia virus
Neoplasm Proteins - isolation & purification
Neoplasm Proteins - metabolism
Phosphatidylinositols - metabolism
Phosphorylation
Protein-Tyrosine Kinases - isolation & purification
Protein-Tyrosine Kinases - metabolism
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Summary: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 MBL 2 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.
Bibliography:ObjectType-Article-1
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(85)91159-3