Characterization of bullet tuna myoglobin with reference to the thermostability-structure relationship

Nobuhiko Ueki, Chau Jen Chow, Yoshihiro Ochiai

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33 Citations (Scopus)


Myoglobin (Mb) was isolated from bullet tuna (Auxis rochei) skeletal muscle and characterized from the viewpoint of the thermostability-structure relationship. Differential scanning calorimetry (DSC) measurement showed that the thermostability of bullet tuna Mb was the lowest among all the scombridae fish Mbs so far examined. The highest value (72.8°C) of melting temperature (Tm) was obtained at pH 6.52. α-Helical content at 10°C was 34.5%, clearly lower than that of horse Mb (55.3%). The amino acid sequence was then deduced by cloning cDNA which encodes bullet tuna Mb. Bullet tuna Mb consisted of 147 amino acids, and the sequence identity was very close to that of skipjack (Katsuwonus pelamis) Mb (91.8%). A few amino acid substitutions, which could be involved in stability difference of Mb, were recognized. By mass spectrometry of lysyl endoproteinase digest of Mb, the N-terminus was found to be acetylated like that of other fish Mbs.

Original languageEnglish
Pages (from-to)4968-4975
Number of pages8
JournalJournal of Agricultural and Food Chemistry
Issue number12
Publication statusPublished - 2005 Jun 15
Externally publishedYes


  • Amino acid sequence
  • Bullet tuna
  • CD
  • CDNA cloning
  • DSC
  • Myoglobin
  • Thermostability

ASJC Scopus subject areas

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)


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