title: Immunoaffinity purification and identification of the molecular chaperone calnexin.
abstract: We have developed a method for the immunoaffinity purification of calnexin, an endoplasmic reticulum molecular chaperone, and analyzed the molecular weight of purified calnexin using matrix-assisted laser adsorption ionization time of flight mass spectrometry (MALDI TOF-MS). Calnexin was thereby found to have a molecular weight of 66.1 x 10(3), which is nearly identical to the molecular weight estimated from the protein sequence.
authors.affiliation: Faculty of Agriculture, Iwate University, Morioka, Japan. yamashit@iwate-u.ac.jp
authors.forename: T
authors.initials: T
authors.lastname: Yamashita
authors.forename: E
authors.initials: E
authors.lastname: Kiyoki
authors.forename: Y
authors.initials: Y
authors.lastname: Tomita
authors.forename: H
authors.initials: H
authors.lastname: Taira
mesh_terms: D002135:Calcium-Binding Proteins / Q000302:isolation & purification*; D037281:Calnexin; D018832:Molecular Chaperones / Q000302:isolation & purification*; D008970:Molecular Weight; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D002135:Calcium-Binding Proteins; D018832:Molecular Chaperones; D037281:Calnexin