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| http://purl.uniprot.org/citations/2174051 | http://www.w3.org/2000/01/rdf-schema#comment | "Phosphoinositide 3-kinase was purified 27,000-fold from rat liver. The enzyme was purified by acid precipitation of the cytosol followed by chromatography on DEAE-Sepharose, S-Sepharose, hydroxylapatite, Mono-Q, and Mono-S columns. When analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the purified phosphoinositide 3-kinase preparation contained an 85-kDa protein and a protein doublet of approximately 110 kDa. The 85- and 110-kDa proteins focus together on native isoelectric focusing gels and are cross-linked by dithiobis(succinylamide propionate), showing that the 110- and 85-kDa proteins are a complex. The apparent size of the native enzyme, as determined by gel filtration, is 190 kDa. The 85-kDa subunit is the same protein previously shown to associate with polyoma virus middle T antigen and the platelet-derived growth factor receptor (Kaplan, D. R., Whitman, M., Schaffhausen, B., Pallas, D. C., White, M., Cantley, L., and Roberts, T. M. (1987) Cell 50, 1021-1029). The two proteins co-migrate on two-dimensional gels; and, using a Western blotting procedure, 32P-labeled middle T antigen specifically blots the 85-kDa protein. The purified enzyme phosphorylates phosphatidylinositol, phosphatidylinositol 4-phosphate, and phosphatidylinositol 4,5-bisphosphate. The apparent Km values for ATP were found to be 60 microM with phosphatidylinositol 4-phosphate or phosphatidylinositol 4,5-bisphosphate as the substrate. The apparent Km for phosphatidyinositol is 60 microM, for phosphatidylinositol 4-phosphate is 9 microM, and for phosphatidylinositol 4,5-bisphosphate is 4 microM. The maximum specific activity using phosphatidylinositol as the substrate is 0.8 mumol/mg/min. The enzyme requires Mg2+ with an optimum of 5 mM. Substitution of Mn2+ for Mg2+ results in only approximately 10% of the Mg2(+)-dependent activity. Physiological calcium concentrations have no effect on the enzyme activity. Phosphoinositide 3-kinase has a broad pH optimum around 7."xsd:string |
| http://purl.uniprot.org/citations/2174051 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(17)45429-9"xsd:string |
| http://purl.uniprot.org/citations/2174051 | http://purl.uniprot.org/core/author | "Cantley L.C."xsd:string |
| http://purl.uniprot.org/citations/2174051 | http://purl.uniprot.org/core/author | "Auger K.R."xsd:string |
| http://purl.uniprot.org/citations/2174051 | http://purl.uniprot.org/core/author | "Schaffhausen B.S."xsd:string |
| http://purl.uniprot.org/citations/2174051 | http://purl.uniprot.org/core/author | "Carpenter C.L."xsd:string |
| http://purl.uniprot.org/citations/2174051 | http://purl.uniprot.org/core/author | "Cohen B."xsd:string |
| http://purl.uniprot.org/citations/2174051 | http://purl.uniprot.org/core/author | "Duckworth B.C."xsd:string |
| http://purl.uniprot.org/citations/2174051 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
| http://purl.uniprot.org/citations/2174051 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/2174051 | http://purl.uniprot.org/core/pages | "19704-19711"xsd:string |
| http://purl.uniprot.org/citations/2174051 | http://purl.uniprot.org/core/title | "Purification and characterization of phosphoinositide 3-kinase from rat liver."xsd:string |
| http://purl.uniprot.org/citations/2174051 | http://purl.uniprot.org/core/volume | "265"xsd:string |
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