酵母のプロタミンキナーゼ : 動物組織のCa^<2+>および環状ヌクレオチド依存性蛋白質リン酸化酵素との比較研究
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概要
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A protein kinase which phosphorylates preferentially protamine was purified about 250-fold from soluble fraction of baker's yeast by streptomycin treatment, followed by ammonium sulfate fractionation, DEAE-cellulose column chromatography, second ammonium sulfate fractionation, hydroxyl apatite column chromatography, and gel filtration on a Sephadex G-75 column. Histone was about 5% as active as protamine in the reaction rate. This enzyme was independent of cyclic nucleotides and clearly distinguished from cyclic AMP-dependent protein kinase as well as from casein kinase. Km value for ATP was 5×10^<-6>M. The optimum pH was 6.0 to 8.0. The isoelectric point was 5.6. The optimum concentration of Mg^<2+> was 10 to 20mM. These characteristics appear to be similar to those described for a Ca^<2+>-activated, phospholipid-dependendent protein kinase recently found in various mammalian tissues (Takai, Y. et al. : J. Biol. Chem. 254, 3692 (1979)), although the exact relation of these two enzymes remains to be explored.
- 神戸大学の論文