Mis-folded ribonucleaseA (RNaseA) could be refolded by the use of microspheres onto which sulfhydryl and disulfide groups were introduced. Modified microspheres were first added to a mis-folded RNaseA aqueous solution. After incubation, proteins were separated from the solution by centrifugation and the enzymatic activity of recovered RNaseA was measured. The refolding was clearly induced by the modified microspheres. On the contrary, virtually no refolding was observed on the unmodified microspheres. Possibly, sulfhydryl groups on the microsphere can preferentially attack disulfide bonds in mis-folded RNaseA, and this attack can trigger protein refolding through thiol-disulfide exchange reactions at the microsphere-protein interface. Copyright (C) 1999 Elsevier Science B.V. All rights reserved.
|ジャーナル||Colloids and Surfaces A: Physicochemical and Engineering Aspects|
|出版ステータス||Published - 1999 8 15|
|イベント||Proceedings of the 1997 7th Iketani Conference - International Symposium on Advanced Technology of Fine Particles - Yokohama, Jpn|
継続期間: 1997 10 12 → 1997 10 16
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