Binding shift assay of parvalbumin, calmodulin and carbonic anhydrase by high-performance capillary electrophoresis.
Shifts in mobility caused by binding of Ca2+ to calmodulin and parvalbumin were studied using high-performance capillary electrophoresis in a Tris-glycine buffer, rather than conventional polyacrylamide gel electrophoresis which requires larger amounts of sample and longer assay time. A Zn(2+)-binding protein, carbonic anhydrase, also showed a partial shift in mobility following Zn(2+)-binding.
Kajiwara
H
H
National Institute of Agrobiological Resources, Ibaraki, Japan.
Hirano
H
H
Oono
K
K
D002021:Buffers; D002118:Calcium / Q000378:metabolism; D002147:Calmodulin / Q000302:isolation & purification* / Q000378:metabolism; D002256:Carbonic Anhydrases / Q000302:isolation & purification*; D004586:Electrophoresis / Q000379:methods*; D010320:Parvalbumins / Q000302:isolation & purification* / Q000378:metabolism; D012710:Serum Albumin, Bovine; D015032:Zinc / Q000378:metabolism
D002021:Buffers; D002147:Calmodulin; D010320:Parvalbumins; D012710:Serum Albumin, Bovine; D002256:Carbonic Anhydrases; D015032:Zinc; D002118:Calcium