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Purification of A Cl--channel protein of sarcoplasmic reticulum by assaying the channel activity in the planar lipid bilayer system

  • Toru Ide
  • , Hiroto Sakamoto
  • , Takuma Morita
  • , Takahisa Taguchi
  • , Michiki Kasai

研究成果査読

抄録

A Cl- channel protein of sarcoplasmic reticulum (SR) was purified by assaying the channel activity in a planar lipid bilayer system. The light fraction of SR vesicles was solubilized in CHAPS and fractionated by anion exchange, gel filtration, and affinity chromatography with concanavalin A. All fractions in each step were reconstituted into vesicles with asolectin by dialysis and their channel activities were assayed after the vesicles had been fused into a planar lipid bilayer. A 100-kDa protein, different from Ca2+-ATPase, was found to form anion channels.

本文言語English
ページ(範囲)38-44
ページ数7
ジャーナルBiochemical and Biophysical Research Communications
176
1
DOI
出版ステータスPublished - 4月 15 1991
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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