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J. Biol. Chem., Vol. 266, Issue 13, 8108-8114, May, 1991
F Shibasaki, Y Homma and T Takenawa
Two types of phosphatidylinositol (PI) 3-kinase (PI3K) have been purified
6250-fold (PI3KI) and 1250-fold (PI3KII) from the cytosol fraction of
bovine thymus. Purified PI3KI and PI3KII were found to have apparent
molecular masses of 110 and 190 kDa, respectively, by gel filtration. On
the other hand, on sodium dodecyl sulfate-polyacrylamide gel
electrophoresis, while the molecular mass of PI3KI was again estimated as
110 kDa, PI3KII showed two bands with apparent molecular masses of 110 and
85 kDa, suggesting a heterodimer form. Peptide mapping analysis
demonstrated that the 110-kDa protein in PI3KII was the same protein as
PI3KI. The specific activity of PI3KI was calculated as 250 nmol/min/mg of
protein, while that of PI3KII was 50 nmol/min/mg of protein. The product of
PI phosphorylation by PI3KI and PI3KII were confirmed as
phosphatidylinositol 3-phosphate by PartiSphere Sax column chromatography.
The results show that there are two types of PI 3-kinase in bovine thymus.
One exists as a monomer and the other as a heterodimer form. Furthermore,
the biochemical properties of these two PI 3-kinases are markedly
different. These two types of PI 3-kinase may be regulated differently
under physiological conditions.
Two types of phosphatidylinositol 3-kinase from bovine thymus. Monomer and heterodimer form
Department of Biosignal Research, Tokyo Metropolitan Institute of Gerontology, Japan.
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