Probing of membrane topology and stability of sarcoplasmic reticulum Ca(2+)-ATPase and Na+,K+ -ATPase with sequence-specific antibodies.
Møller
J V
JV
Department of Biophysics, University of Aarhus, Denmark.jvm@biophys.aa Department of Biophysics, University of Aarhus, Denmark. jvm@ biophys.aau.dk
Juul
B
B
Falson
P
P
Le Maire
M
M
D000818:Animals; D000906:Antibodies; D001666:Binding Sites, Antibody; D000252:Calcium-Transporting ATPases / Q000737:chemistry* / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D003600:Cytosol / Q000201:enzymology; D004797:Enzyme-Linked Immunosorbent Assay; D007425:Intracellular Membranes / Q000201:enzymology / Q000648:ultrastructure; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology*; D008958:Models, Molecular; D011487:Protein Conformation; D012519:Sarcoplasmic Reticulum / Q000201:enzymology* / Q000648:ultrastructure; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000378:metabolism; D013552:Swine
D000906:Antibodies; D000252:Calcium-Transporting ATPases; D000254:Sodium-Potassium-Exchanging ATPase