Refolding of protein using thiol-carrying latex particles

Hidenobu Shimizu, Keiji Fujimoto, Haruma Kawaguchi

Research output: Contribution to journalConference articlepeer-review

28 Citations (Scopus)


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 languageEnglish
Pages (from-to)421-427
Number of pages7
JournalColloids and Surfaces A: Physicochemical and Engineering Aspects
Issue number1-3
Publication statusPublished - 1999 Aug 15
EventProceedings of the 1997 7th Iketani Conference - International Symposium on Advanced Technology of Fine Particles - Yokohama, Jpn
Duration: 1997 Oct 121997 Oct 16


  • 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


Dive into the research topics of 'Refolding of protein using thiol-carrying latex particles'. Together they form a unique fingerprint.

Cite this