GroEL or nanogel-mediated folding of β-D-galactosidase was examined. Urea-denatured β-D-galactosidase can spontaneously fold upon the dilution into the low urea concentration (about 15 %). In the presence of GroEL or ALP nanogel, folding of β-D-galactosidase was started by following the dilution. About 50 % of β-D-galactosidase recovered to native structure in both systems of GroEL and dodecyl group-bearing pullulan (ALP) nanogel recovered to native structure. The addition of ATP for GroEL has little effect on refolding. In contrast, the folding was arrested in the presence of CHP nanogels. Even by the addition of methyl-β-cyclodextrin for CHP nanogels, only 15 % of β-D-galactosidase activity recovered. Hydrophobie groups in the nanogels significantly affect chaperon-like activity.
|出版ステータス||Published - 2005 12 1|
|イベント||54th SPSJ Annual Meeting 2005 - Yokohama, Japan|
継続期間: 2005 5 25 → 2005 5 27
|Other||54th SPSJ Annual Meeting 2005|
|Period||05/5/25 → 05/5/27|
ASJC Scopus subject areas