Detection of an endothelin-1-binding protein complex by low temperature SDS-PAGE.
We found that the complex of ET-1 and its binding protein was stable enough to be separated by SDS-PAGE when electrophoresis was run at a low temperature. Cross-linking was not necessary for the detection of [125I]-ET-1 and its binding protein complex by autoradiography. This simple method could be used in qualitative (estimation of apparent molecular weight of ET-1 binding protein) and quantitative (determination of relative content of ET-binding protein) analysis of the ET-binding protein complex. ET-binding protein complexes of various animal species and organs were investigated by this method.
Takasuka
T
T
Department of Molecular Genetics, Nippon Roche Research Center, Kamakura, Japan.
Horii
I
I
Furuichi
Y
Y
Watanabe
T
T
D000818:Animals; D001345:Autoradiography; D002793:Cholic Acids; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D016232:Endothelins / Q000302:isolation & purification / Q000378:metabolism*; D005260:Female; D006168:Guinea Pigs; D006801:Humans; D007457:Iodine Radioisotopes; D007700:Kinetics; D051379:Mice; D008861:Microsomes / Q000378:metabolism; D008970:Molecular Weight; D009928:Organ Specificity; D011247:Pregnancy; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000302:isolation & purification / Q000378:metabolism*; D017466:Receptors, Endothelin
D002793:Cholic Acids; D016232:Endothelins; D007457:Iodine Radioisotopes; D011956:Receptors, Cell Surface; D017466:Receptors, Endothelin; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate