Thermal Denaturation and Renaturation of γ-Glutamyltranspeptidase of <i>Escherichia coli</i>

• HO Thao Van

  Division of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology

• KAMEI Kaeko

  Division of Biomolecular Engineering, Graduate School of Science and Technology, Kyoto Institute of Technology

• WADA Kei

  Organization for Promotion of Tenure Track, University of Miyazaki

• FUKUYAMA Keiichi

  Department of Biological Sciences, Graduate School of Science, Osaka University

• SUZUKI Hideyuki

  Division of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology

Bibliographic Information

Other Title

• Thermal Denaturation and Renaturation of γ-Glutamyltranspeptidase of Escherichia coli

Abstract

Heat-treated γ-glutamyltranspeptidase of Escherichia coli recovered enzymatic activity after incubation at 4 °C, while heat-treated γ-glutamyltranspeptidase of Bacillus subtilis did not. Fluorescent spectra, CD spectra, and native polyacrylamide gel electrophoresis analysis suggested that the dimer of E. coli γ-glutamyltranspeptidase was separated into protomers by heat-treatment, but was renatured by incubation at 4 °C.

Journal

• Bioscience, Biotechnology, and Biochemistry

  Bioscience, Biotechnology, and Biochemistry 77 (2), 409-412, 2013

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• γ-glutamyltranspeptidase
• denaturation
• renaturation

Details

• CRID: 1390282681456814592
• NII Article ID: 10031164753
• NII Book ID: AA10824164
• DOI: 10.1271/bbb.120780
• COI: 1:STN:280:DC%2BC3szmsFKrtQ%3D%3D
• ISSN: 13476947
• ISSN: 09168451
• NDL BIB ID: 024296076
• PubMed: 23391932
• Web Site: http://id.ndl.go.jp/bib/024296076
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I024296076
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed