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Folding and Unfolding Behavior of Carboxypeptidase Y Inhibitor (IC) Induced by Temperature and Pressure

  • Joji Mima
  • Yo Sato
  • Michiko Kato
  • Rikimaru Hayashi
Conference paper

Abstract

Carboxypeptidase Y (CPY) inhibitor, IC, is a heat-stable proteinase inhibitor produced by the yeast Saccharomyces cerevisiae [Matern, H., Hoffmann, M., and Holzer, H. (1974) Proc. Nat. Acad. Sci. USA 71, 4874–4878]. The heat- and pressure-induced unfolding of IC was investigated by means of fluorescence and circular dichroism spectroscopy, in order to better understand the structural basis for its high heat-stability. The heat-induced denaturation showed a two-state transition and was irreversible, while the pressure-induced denaturation showed a multiple-state transition and was completely reversible. The β-sheet of IC was converted into α-helix and random coil structures after heat treatment at 75 ºC whereas the secondary structure content remained unchanged after a pressure treatment at 400 MPa. Thus, it appears that the β-sheet-rich structure of IC is important for its structural stability.

Keywords

Pressure Treatment Secondary Structure Content Random Coil Structure General Serine Proteinase Cular Dichroism 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 2003

Authors and Affiliations

  • Joji Mima
    • 1
  • Yo Sato
    • 1
  • Michiko Kato
    • 1
  • Rikimaru Hayashi
    • 1
  1. 1.Division of Applied Life Sciences, Graduate School of AgricultureKyoto UniversitySakyo-ku, KyotoJapan

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