Immunoaffinity purification and identification of the molecular chaperone calnexin.
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.
Yamashita
T
T
Faculty of Agriculture, Iwate University, Morioka, Japan. yamashit@iwate-u.ac.jp
Kiyoki
E
E
Tomita
Y
Y
Taira
H
H
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
D002135:Calcium-Binding Proteins; D018832:Molecular Chaperones; D037281:Calnexin