Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 421-427 |
| Number of pages | 7 |
| Journal | Colloids and Surfaces A: Physicochemical and Engineering Aspects |
| Volume | 153 |
| Issue number | 1-3 |
| DOIs | |
| Publication status | Published - 1999 Aug 15 |
| Event | Proceedings of the 1997 7th Iketani Conference - International Symposium on Advanced Technology of Fine Particles - Yokohama, Jpn Duration: 1997 Oct 12 → 1997 Oct 16 |
Keywords
- Polymeric microsphere
- Protein refolding
- RibonucleaseA
- Sulfhydryl group
- Thiol-disulfide exchange reaction
ASJC Scopus subject areas
- Surfaces and Interfaces
- Physical and Theoretical Chemistry
- Colloid and Surface Chemistry