Characterization of refolded hen lysozyme variant lacking two outside disulfide bonds

Takatoshi Ohkuri, Taiji Imoto, Tadashi Ueda

Research output: Contribution to journalArticle

Abstract

We characterized a refolded hen lysozyme variant containing only two SS-bonds, C64-C80 and C76-C94 (4CAHEL). From CD spectra and its activity, it was found that the refolded 4CAHEL has a structural topology analogous to wild-type lysozyme (WTHEL). Moreover, the refolded 4CAHEL showed no thermal transition, indicating that it had a character like a molten globule.

Original languageEnglish
Pages (from-to)1206-1208
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume69
Issue number6
DOIs
Publication statusPublished - Jun 1 2005

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disulfide bonds
Muramidase
lysozyme
Disulfides
hens
Enzymes
topology
Molten materials
Hot Temperature
Topology
heat
C 76

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Biotechnology
  • Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Chemistry (miscellaneous)
  • Applied Microbiology and Biotechnology
  • Food Science

Cite this

Characterization of refolded hen lysozyme variant lacking two outside disulfide bonds. / Ohkuri, Takatoshi; Imoto, Taiji; Ueda, Tadashi.

In: Bioscience, Biotechnology and Biochemistry, Vol. 69, No. 6, 01.06.2005, p. 1206-1208.

Research output: Contribution to journalArticle

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