TY - JOUR
T1 - Purification of A Cl--channel protein of sarcoplasmic reticulum by assaying the channel activity in the planar lipid bilayer system
AU - Ide, Toru
AU - Sakamoto, Hiroto
AU - Morita, Takuma
AU - Taguchi, Takahisa
AU - Kasai, Michiki
PY - 1991/4/15
Y1 - 1991/4/15
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(91)90886-C
DO - 10.1016/0006-291X(91)90886-C
M3 - Article
C2 - 1708250
AN - SCOPUS:0025826265
VL - 176
SP - 38
EP - 44
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -