Equilibrium Study on Interactions between Proteins and Bile-Salt Micelles by Micellar Electrokinetic Chromatography.

• SAITOH Tohru

  Faculty of Engineering, Hokkaido University

• FUKUDA Teruyuki

  Faculty of Engineering, Hokkaido University

• TANI Hirofumi

  Faculty of Engineering, Hokkaido University

• KAMIDATE Tamio

  Faculty of Engineering, Hokkaido University

• WATANABE Hiroto

  Faculty of Engineering, Hokkaido University

Abstract

Interactions between proteins and bile-salt micelles were evaluated on the basis of the binding constants, which were obtained from the migration of proteins in micellar electrokinetic chromatography. The binding constants, K_b=[P_b]/ ([P_w][B]), where [P_b] is the concentration of a protein binding with a bile-salt, [P_w] free protein concentration, and [B] the concentration of bile salt present in the micelles, were successfully determined from the slope of a linear curve of the capacity factor (k′) of the protein against [B]. The binding constants were almost identical to those obtained by a gel- filtration method. The value of K_b increased with increasing the hydrophobicity of the bile salt or that of the protein.

Journal

• Analytical Sciences

  Analytical Sciences 12 (4), 569-573, 1996

  The Japan Society for Analytical Chemistry

Keywords

• Protein
• bile-salt micelle
• binding constant
• micellar electrokinetic chromatography

Details

• CRID: 1390282679233254656
• NII Article ID: 10002408960
• NII Article ID: 130003416613
• NII Book ID: AA10500785
• DOI: 10.2116/analsci.12.569
• COI: 1:CAS:528:DyaK28XkvFGitbs%3D
• ISSN: 13482246
• ISSN: 09106340
• HANDLE: 2115/71708
• Web Site: https://link.springer.com/content/pdf/10.2116/analsci.12.569.pdf
• Web Site: https://link.springer.com/article/10.2116/analsci.12.569/fulltext.html
• Web Site: http://www.jstage.jst.go.jp/article/analsci1985/12/4/12_4_569/_pdf
• Text Lang: en
• Data Source:
  • JaLC
  • IRDB
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed