Purification and characterization of golgi membrane-bound nucleoside diphosphatase from suspension-cultured cells of sycamore (acer pseudoplatanus L.)

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概要

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• Inosine diphosphatase (IDPase) isoforms associated with Golgi membranes were studied in sycamore cell culture. These enzyme isoforms were solubilized with Triton X-100 and purified by chromatography using DEAE-Toyopearl and SOURCE-S columns. The isoforms were separated into two distinguishable fractions (peak 1 and 2) by SOURCE-S column chromatography. Furthermore the peak 1 contained at least two isoform bands detected by native-PAGE analysis. The apparent molecular sizes of these three isoforms were estimated by both gel filtration and SDS-PAGE to be 50 kDa, indicating that the Golgi membrane-bound IDPase has a monomeric structure. These IDPase isoforms required divalent cations (Ca2+, Mg2+, Co2+, Mn2+) for their hydrolyzing activity, and were inhibited by ATP. IDP, UDP, and GDP were effective substrates for these enzymes. It is clearly indicated that the sycamore Golgi membrane-bound IDPase is a nucleoside diphosphatase.

• 日本植物細胞分子生物学会の論文
• 2001-12-01

著者

• Mikami Satoshi

  Laboratories Of Molecular Life Science Graduate School Of Science And Technology Niigata University

• Mitsui Toshiaki

  Graduate School of Science and Technology, Niigata University

• Hori Hidetaka

  Laboratories Of Molecular Life Science Graduate School Of Science And Technology Niigata University

• Mitsui Toshiaki

  Laboratories Of Molecular Life Science Graduate School Of Science And Technology Niigata University

• Suganuma Ryo

  Laboratories Of Molecular Life Science Graduate School Of Science And Technology Niigata University

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