Nondenaturing solubilization of β2 microglobulin from inclusion bodies by L-arginine

Mitsuo Umetsu, Kouhei Tsumoto, Shigeki Nitta, Tadafumi Adschiri, Daisuke Ejima, Tsutomu Arakawa, Izumi Kumagai

Research output: Contribution to journalArticlepeer-review

57 Citations (Scopus)


Expression of β2 microglobulin (β2m) in Escherichia coli resulted in formation of inclusion bodies. Attenuated total reflectance Fourier transform infrared analysis suggested a native-like secondary structure of β2m in the inclusion bodies. Nondenaturing solubilization of the native-like β2m from inclusion bodies was achieved using l-arginine solution, which enables an efficient recovery of β2m with little aggregation. Greater β2m solubilization from inclusion bodies was obtained at higher temperatures. Low-temperature solubilization yielded β2m with fluorescence properties identical to those of native β2m, but its secondary structure was slightly nonnative. Solubilization at moderate temperature gave β2m with an apparently native structure. We propose an efficient nondenaturing solubilization method combining L-arginine and moderate temperature.

Original languageEnglish
Pages (from-to)189-197
Number of pages9
JournalBiochemical and biophysical research communications
Issue number1
Publication statusPublished - 2005 Mar 4


  • Inclusion body
  • Nondenaturing reagent
  • Oligomerization
  • Solubilizing reagent
  • Spectroscopic analysis

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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