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 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.
D019870:1-Phosphatidylinositol 4-Kinase; D000818:Animals; D002845:Chromatography; D008099:Liver / Q000201:enzymology*; D008566:Membranes / Q000201:enzymology; D051379:Mice; D008970:Molecular Weight; D010716:Phosphatidylinositols / Q000096:biosynthesis* / Q000378:metabolism; D010770:Phosphotransferases / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
D010716:Phosphatidylinositols; D010770:Phosphotransferases; D019870:1-Phosphatidylinositol 4-Kinase