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

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)38-44
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume176
Issue number1
DOIs
Publication statusPublished - Apr 15 1991
Externally publishedYes

Fingerprint

Lipid bilayers
Lipid Bilayers
Sarcoplasmic Reticulum
Purification
Anions
Affinity chromatography
Dialysis
Calcium-Transporting ATPases
Concanavalin A
Affinity Chromatography
Gel Chromatography
Ion exchange
Proteins
Gels
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate
asolectin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Purification of A Cl--channel protein of sarcoplasmic reticulum by assaying the channel activity in the planar lipid bilayer system. / Ide, Toru; Sakamoto, Hiroto; Morita, Takuma; Taguchi, Takahisa; Kasai, Michiki.

In: Biochemical and Biophysical Research Communications, Vol. 176, No. 1, 15.04.1991, p. 38-44.

Research output: Contribution to journalArticle

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