Dimerization characteristics of the 94-kDa glucose-regulated protein.

@article{Nemoto1996DimerizationCO,
  title={Dimerization characteristics of the 94-kDa glucose-regulated protein.},
  author={Tadashi Nemoto and Tadao Matsusaka and Motonori Ota and Tetsuo Takagi and David B. Collinge and Haidee Walther-Larsen},
  journal={Journal of biochemistry},
  year={1996},
  volume={120 2},
  pages={249-56}
}
The 94-kDa glucose-regulated protein (GRP94) is a member of the 90-kDa heat-shock protein (HSP90) family. In this study, we expressed the barley (Hordeum vulgare L.) GRP94 and the alpha isoform of human HSP90 (HSP90 alpha) in Escherichia coli and compared their dimer-forming abilities. Native polyacrylamide gel electrophoresis revealed that GRP94 (amino acids 69-809) and the full-length form of HSP90 alpha existed in the dimeric state. The C-terminal 326 amino acids of GRP94 or the C-terminal… CONTINUE READING