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2011 Fiscal Year Final Research Report

Establishment of high concentration Refolding of unstable protein

Research Project

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Project/Area Number 21580119
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Applied biochemistry
Research InstitutionSojo University

Principal Investigator

MATSUMOTO Toshihiko  崇城大学, 生物生命学部, 准教授 (60133568)

Co-Investigator(Kenkyū-buntansha) MATSUMOTO Toshihiko  崇城大学, 生物生命学部, 准教授 (60133568)
YAMAURA Izumi  崇城大学, 生物生命学部, 教授 (30133565)
Project Period (FY) 2009 – 2011
Keywords再生 / フォルディング / 安定化剤 / 可溶化剤 / 不安定蛋白質
Research Abstract

Earlier, we formally established an effective refolding procedure for a protein by gradient removal of a solubilizer such as urea. However, this procedure was less effective for unstable proteins. We developed here an excellent method to add protein stabilizer so as to get reasonable amounts of folded protein under the concentration of solubilizer where the unstable protein does not form aggregate. We examined many stabilizers and found that 60% of a concentrated(2.5 mg/ml) unstable protein can be refolded using 40% glycerol as the best stabilizer. This procedure can be widely applicable for the refolding of unstable proteins.

  • Research Products

    (2 results)

All 2012 2010

All Journal Article (1 results) (of which Peer Reviewed: 1 results) Presentation (1 results)

  • [Journal Article] Refolding of an unstable lysozyme by gradient removal of a solubilizer and gradient addition of a stabilizer2010

    • Author(s)
      Kohyama K, Matsumoto T, and Imoto T
    • Journal Title

      J. Biochem

      Volume: 143巻 Pages: 427-431

    • Peer Reviewed
  • [Presentation] 不安定タンパク質の効率的な再生法の確立2012

    • Author(s)
      保田達哉, 野稲俊宏, 松元俊彦, 安藤祥司, 井本泰治
    • Organizer
      日本農芸化学会
    • Place of Presentation
      京都女子大
    • Year and Date
      2012-03-24

URL: 

Published: 2013-07-31  

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