Structural and thermodynamic characterization of tropomyosin from fast skeletal muscle of bluefin tuna

Ming Chih Huang, Yoshihiro Ochiai, Shugo Watabe

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

Tuna tropomyosin is a mixture of nearly equimolar amounts of two isoforms (designated αand β). cDNA encoding the α form was cloned from bluefin tuna Thunnus thynnus fast skeletal muscle. The full-length cDNA contained 1220 bp, comprising an open reading frame of 855 bp encoding 284 amino acid residues, flanked by 5′-untranslational regions (156 bp) and 3′-untranslational regions (209 bp). The deduced amino acid sequence showed considerably high homology in a range of 93.7-98.6% to those of other vertebrate α-type tropomyosins. In phylogenetic analysis, bluefin tuna tropomyosin showed the closest relationship with the white croaker counterpart. The predicted mass was 32 919 Da, and isoelectric point was 4.50, assuming acetylation of the N-terminus. By differential scanning calorimetry, bluefin tuna tropomyosin gave two major endothermic peaks at 29.3 and 41.5°C, probably caused by the presence of two isoforms. Circular dichroism spectra supported such a unique denaturation profile.

Original languageEnglish
Pages (from-to)667-674
Number of pages8
JournalFisheries Science
Volume70
Issue number4
DOIs
Publication statusPublished - 2004 Aug 1
Externally publishedYes

Keywords

  • Bluefin tuna
  • Primary structure
  • Skeletal muscle
  • Thermostability
  • Tropomyosin
  • cDNA cloning

ASJC Scopus subject areas

  • Aquatic Science

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