Some Characteristics of Membrane-Associated Protein Kinase in Lemna paucicostata
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概要
- 論文の詳細を見る
A protein kinase which phosphorylates histone was isolated from the endoplasmic reticulum-rich fractions of Lemna paucicostata. The enzyme could be solubilized by sonication, and its molecular weight was estimated as 220,000 by Sephacryl S-300 gel filtration. The optimum pH for enzyme activity was 9.0-9.5 and the activity was stimulated by Co^<2+>, Mg^<2+> and Mn^<2+>. Substrate proteins which might be phosphorylated by this protein kinase were also detected in microsomal fractions of Lemna plants.
- 日本植物生理学会の論文
著者
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Fujii Tadashi
Institute of Biological Sciences, University of Tsukuba
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Kato R
Biology Laboratory Faculty Of Education Yamagata University
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Kato Ryoichi
Institute Of Biological Sciences University Of Tsukuba
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Fujii Tadashi
Institute Of Biological Sciences University Of Tsukuba
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Fujii Tadashi
Institute Of Biological Science The University Of Tsukuba
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