Partially purified phosphatidylinositol kinase does not catalyze the formation of phosphatidylinositol-4,5-bisphosphate

Partially purified phosphatidylinositol kinase does not catalyze the formation of phosphatidylinositol-4,5-bisphosphate

The enzyme phosphatidylinositol kinase was partially purified from murine livers. The purification scheme involved solubilization of proteins with Triton X-100 and deoxycholate, followed by gel filtration chromatography in ACA 44, affinity chromatography with Blue Sepharose and hydroxylapatite. The...

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Veröffentlicht in:Biochemical and biophysical research communications 1987-03, Vol.143 (2), p.512-516
Hauptverfasser: Suárez-Quian, Carlos A., O'Shea, John J., Klausner, Richard D.
Format: Artikel
Sprache:eng
Schlagworte:
1-Phosphatidylinositol 4-Kinase
Animals
Chromatography
Liver - enzymology
Membranes - enzymology
Mice
Molecular Weight
Phosphatidylinositols - biosynthesis
Phosphatidylinositols - metabolism
Phosphotransferases - isolation & purification
Phosphotransferases - metabolism
Substrate Specificity
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Zusammenfassung:The enzyme phosphatidylinositol kinase was partially purified from murine livers. The purification scheme involved solubilization of proteins with Triton X-100 and deoxycholate, followed by gel filtration chromatography in ACA 44, affinity chromatography with Blue Sepharose and hydroxylapatite. The purification achieved from membranes was 490 fold. We found that partially purified phosphatidylinositol kinase was unable to catalyze the formation of phosphatidylinositol-4,5-bisphosphate.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(87)91383-0