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Plant and Cell Physiology, 1985, Vol. 26, No. 7 1379-1386
© 1985

Article

Some Characteristics of Membrane-Associated Protein Kinase in Lemna paucicostata

Ryoichi Kato1 and Tadashi Fujii

Institute of Biological Sciences, University of Tsukuba Sakwa-mura, Ibaraki 305, Japan

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 Co2$, Mg2$ and Mn2$. Substrate proteins which might be phosphorylated by this protein kinase were also detected in microsomal fractions of Lemna plants.

1 Present address: Advanced Research Laboratory, HITACHI LTD., Kokubunji, Tokyo 185, Japan.

(Received March 9, 1985; Accepted August 7, 1985)
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