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KMID : 0368419900330040325
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Journal of Plant Biology
1990 Volume.33 No. 4 p.325 ~ p.332
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Purification and Characterization of ATPases and Phosphatase of Light Membrane Vesicles Isolated from Cucurbita pepo
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Oh Seung-Eun
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Abstract
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Light membrane vesicles were isolated from the zucchini hypocotyl by floatation on ficoll density gradients and the proteins were solubilized with Triton X100. Three ATP-hydrolyzing enzymes were partially purified by ion-exchange and gel filtration chromatography and isoelectric focusing. There are plasma membrane-type ATPase whose activity was inhibited by vanadate but not by nitrate, tonoplast-type ATPase which was sensitive to nitrate but insensitive to vanadate and one having a phosphatase activity with a pI value different from that of an acid phosphatase. A fraction was obtained after DEAE-ion-exchange chromatography crossreacting with polyclonal antibodies against Ca^2+-ATPase from human erythrocytes.
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