%0 Journal Article %1 Liu_1991_13 %A Liu, Q. Y. %A Lai, F. A. %A Shen, W. K. %A Meissner, G. %A Strauss, H. C. %D 1991 %J FEBS Lett %K 1936241 Animals, Centrifugation, Channels, Density Dogs, Electrophoresis, Gel, Gov't, Gradient, Myocardium, P.H.S., Polyacrylamide Potassium Research Reticulum, Sarcoplasmic Solubility, Support, U.S. %N 1 %P 13--16 %T Reconstitution of the solubilized cardiac sarcoplasmic reticulum potassium channel. Identification of a putative Mr approximately 80 kDa polypeptide constituent. %U http://dx.doi.org/10.1016/0014-5793(91)81092-M %V 291 %X Recent evidence has indicated that potassium ion movement through sarcoplasmic reticulum (SR) K$^+$ channels is an important countercurrent for Ca$^2+$ release from SR. We used Chaps-solubilized SR vesicles and sucrose density gradient centrifugation to identify components of the canine cardiac SR K$^+$ channel. To overcome the difficulty of the absence of a high-affinity specific ligand, we have successfully applied the planar lipid bilayer reconstitution technique to identify and functionally assay for the solubilized SR K$^+$ channel. We found that Chaps solubilization of the channel did not change the protein's functional properties. The cardiac SR K$^+$ channel sediments as a 15-20S protein complex. A polypeptide of Mr approximately 80 kDa was found to specifically comigrate with the 15-20S gradient fractions and might be a major constituent of the cardiac SR K$^+$ channel.

@article{Liu_1991_13, abstract = {Recent evidence has indicated that potassium ion movement through sarcoplasmic reticulum (SR) {K}$^{+}$ channels is an important countercurrent for {C}a$^{2+}$ release from SR. We used Chaps-solubilized SR vesicles and sucrose density gradient centrifugation to identify components of the canine cardiac SR {K}$^{+}$ channel. To overcome the difficulty of the absence of a high-affinity specific ligand, we have successfully applied the planar lipid bilayer reconstitution technique to identify and functionally assay for the solubilized SR {K}$^{+}$ channel. We found that Chaps solubilization of the channel did not change the protein's functional properties. The cardiac SR {K}$^{+}$ channel sediments as a 15-20S protein complex. A polypeptide of Mr approximately 80 kDa was found to specifically comigrate with the 15-20S gradient fractions and might be a major constituent of the cardiac SR {K}$^{+}$ channel.}, added-at = {2009-06-03T11:20:58.000+0200}, author = {Liu, Q. Y. and Lai, F. A. and Shen, W. K. and Meissner, G. and Strauss, H. C.}, biburl = {https://www.bibsonomy.org/bibtex/2bfb1a060372c1e66496a46ad46ef50d1/hake}, description = {The whole bibliography file I use.}, file = {Liu_1991_13.pdf:Liu_1991_13.pdf:PDF}, interhash = {c06bc02c7c1db92d48d0a72972e53939}, intrahash = {bfb1a060372c1e66496a46ad46ef50d1}, journal = {F{EBS} Lett}, key = 211, keywords = {1936241 Animals, Centrifugation, Channels, Density Dogs, Electrophoresis, Gel, Gov't, Gradient, Myocardium, P.H.S., Polyacrylamide Potassium Research Reticulum, Sarcoplasmic Solubility, Support, U.S.}, month = Oct, number = 1, pages = {13--16}, pmid = {1936241}, timestamp = {2009-06-03T11:21:20.000+0200}, title = {Reconstitution of the solubilized cardiac sarcoplasmic reticulum potassium channel. Identification of a putative Mr approximately 80 kDa polypeptide constituent.}, url = {http://dx.doi.org/10.1016/0014-5793(91)81092-M}, volume = 291, year = 1991 }