Characterization of Protein Phosphatase 2A Acting on Phosphorylated Plasma Membrane Aquaporin of Tulip Petals

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概要

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• A protein phosphatase holo-type enzyme (38, 65, and 75 kDa) preparation and a free catalytic subunit (38 kDa) purified from tulip petals were characterized as protein phosphatase 2A (PP2A) by immunological and biochemical approaches. The plasma membrane containing the putative plasma membrane aquaporin (PM-AQP) was prepared from tulip petals, phosphorylated in vitro, and used as the substrate for both of the purified PP2A preparations. Although both preparations dephosphorylated the phosphorylated PM-AQP at 20 °C, only the holo-type enzyme preparation acted at 5 °C on the phosphorylated PM-AQP with higher substrate specificity, suggesting that regulatory subunits are required for low temperature-dependent dephosphorylation of PM-AQP in tulip petals.

• 社団法人 日本農芸化学会の論文
• 2004-05-23

著者

• Ishikawa Tomohiro

  Department Of Agricultural Chemistry School Of Agriculture Nagoya University

• Shibata Hiroyuki

  Institute For Chemical Research Kyoto University

• ISHIKAWA Takahiro

  Faculty of Agriculture, Gifu University

• Ishikawa T

  Fac. Of Life And Environmental Sci. Shimane Univ.

• AZAD Abul

  Faculty of Life and Environmental Sciences, Shimane University

• SAWA Yoshihiro

  Faculty of Life and Environmental Sciences, Shimane University

• SHIBATA Hitoshi

  Faculty of Life and Environmental Sciences, Shimane University

• Kalam Azad

  Faculty Of Life And Environmental Sciences Shimane University

• Azad Abul

  Faculty Of Agriculture Yamagata University

• Shibata H

  Dept. Life Environ. Sci. Shimane Univ.

• Sawa Yoshihiro

  Dept. Life Environ. Sci. Shimane Univ.

• Sawa Yoshihiro

  Faculty Of Life And Environmental Science Shimane University

• Sawa Yoshihiro

  Dept. Appl. Biosci. And Biotech. Fac. Life And Environ. Sci. Shimane Univ.

• Sakamoto Yoko

  Department Of Food Science And Technology College Of Bioresouce Sciences Nihon University

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