Some Characteristics of Protein Kinases in Lemna paucicostata |
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Authors: | Kato, Ryoichi Uno, Isao Ishikawa, Tatsuo Fujii, Tadashi |
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Affiliation: | 1Institute of Biological Sciences, University of Tsukuba Sakura-mura, Ibaraki 305, Japan 2Institute of Applied Microbiology, University of Tokyo Bunkyo-ku, Tokyo 113, Japan |
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Abstract: | The three protein kinases of Lemna paucicostata that are separableby DEAE-Sephacel chromatography have been designated PI, PIIand PIII [Kato et al. (1983) Plant & Cell Physiol. 24: 841].The optimum pH for the PI and PII enzymes was 7.5 and for thePHI enzyme 7.0. The activities of these enzymes were stimulatedby divalent cations, the maximum stimulation being producedby 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 weightsof the PI and PII enzymes did not change after incubation withcAMP even though their activities were regulated by this compound. (Received October 17, 1983; ) |
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