Refolding of protein using thiol-carrying latex particles

Hidenobu Shimizu, Keiji Fujimoto, Haruma Kawaguchi

研究成果: Conference article査読

28 被引用数 (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.

ジャーナルColloids and Surfaces A: Physicochemical and Engineering Aspects
出版ステータスPublished - 1999 8月 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月 121997 10月 16

ASJC Scopus subject areas

  • 表面および界面
  • 物理化学および理論化学
  • コロイド化学および表面化学


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