Quantitative Analysis of Protein Association System Using High-Pressure Electrophoresis

• ISHIGURO Ryo

  Department of Chemistry and Biomolecular Science, Gifu University

• FUJISAWA Tetsuro

  Department of Chemistry and Biomolecular Science, Gifu University

Bibliographic Information

Other Title

• 高圧力電気泳動法を用いたタンパク質解離会合系の定量的解析
• コウアツリョク デンキ エイドウホウ オ モチイタ タンパクシツ カイリ カイゴウケイ ノ テイリョウテキ カイセキ

Abstract

High-pressure electrophoresis was designed to investigate the association system of proteins quantitatively. In this methodology, pressure and temperature precisely perturbs the association equilibrium of supermolecular protein assembly, whose decomposed fractions can be in-situ analyzed by native polyacrylamide gel electrophoresis (PAGE). The bands of these fractions allow us not only to unravel the elementary process of assembly formation but also to quantify various volumetric properties including thermal expansion change of each process. In this article, we report its application to the problem of amyloid protofibril formation.<br>

Journal

• The Review of High Pressure Science and Technology

  The Review of High Pressure Science and Technology 27 (1), 26-32, 2017

  The Japan Society of High Pressure Science and Technology

Keywords

• high-pressure native polyacrylamide gel electrophoresis
• supermolecular protein assembly
• association equilibrium
• thermodynamic analysis
• volumetric properties
• thermal expansion change

Details

• CRID: 1390001204381302528
• NII Article ID: 130006792996
• NII Article ID: 40021190521
• NII Book ID: AN10452913
• DOI: 10.4131/jshpreview.27.26
• ISSN: 13481940
• ISSN: 0917639X
• NDL BIB ID: 028171987
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I028171987
• Web Site: https://www.jstage.jst.go.jp/article/jshpreview/27/1/27_26/_pdf
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed