title: Binding shift assay of parvalbumin, calmodulin and carbonic anhydrase by high-performance capillary electrophoresis.
abstract: 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.
authors.affiliation: National Institute of Agrobiological Resources, Ibaraki, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Kajiwara
authors.forename: H
authors.initials: H
authors.lastname: Hirano
authors.forename: K
authors.initials: K
authors.lastname: Oono
mesh_terms: 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
chemical_list: D002021:Buffers; D002147:Calmodulin; D010320:Parvalbumins; D012710:Serum Albumin, Bovine; D002256:Carbonic Anhydrases; D015032:Zinc; D002118:Calcium