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Immunoaffinity purification and identification of the molecular chaperone calnexin
T Yamashita1, E Kiyoki, Y Tomita
1Faculty of Agriculture, Iwate University, Morioka, Japan. yamashit@iwate-u.ac.jp
Bioscience, Biotechnology, and Biochemistry
|September 29, 1999
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.