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 fractioned 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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Chloride Channels
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Chromatography, Affinity
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Chromatography, DEAE-Cellulose
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Chromatography, Gel
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Chromatography, High Pressure Liquid
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Electric Conductivity
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Electrophoresis, Polyacrylamide Gel
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Ion Channels / physiology
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Lipid Bilayers*
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Membrane Proteins / drug effects
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Membrane Proteins / isolation & purification
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Membrane Proteins / physiology*
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Molecular Weight
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Muscles / physiology
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Rabbits
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Sarcoplasmic Reticulum / physiology*
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Sulfates / pharmacology
Substances
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Chloride Channels
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Ion Channels
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Lipid Bilayers
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Membrane Proteins
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Sulfates