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Plant and Cell Physiology, 1984, Vol. 25, No. 5 691-696
© 1984

Article

Some Characteristics of Protein Kinases in Lemna paucicostata

Ryoichi Kato1, Isao Uno2, Tatsuo Ishikawa2 and Tadashi Fujii1

1Institute of Biological Sciences, University of Tsukuba Sakura-mura, Ibaraki 305, Japan
2Institute of Applied Microbiology, University of Tokyo Bunkyo-ku, Tokyo 113, Japan

The three protein kinases of Lemna paucicostata that are separable by DEAE-Sephacel chromatography have been designated PI, PII and PIII [Kato et al. (1983) Plant & Cell Physiol. 24: 841]. The optimum pH for the PI and PII enzymes was 7.5 and for the PHI enzyme 7.0. The activities of these enzymes were stimulated by divalent cations, the maximum stimulation being produced by 5 nw Mg2 $ for PI, by 3 mM Co2 $ for PII and by 1 mM Mn2 $ for PIII. The cytokinins; benzyladenine, kinetin and zeatin, inhibited the activity of the PIII enzyme. The molecular weights of the PI and PII enzymes did not change after incubation with cAMP even though their activities were regulated by this compound.

(Received October 17, 1983; )
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