Thermostability of tropomyosins from the fast skeletal muscles of tropical fish species

Ming Chih Huang; Cheng Linn Lee; Yoshihiro Ochiai; Shugo Watabe

doi:10.1007/s10695-019-00632-7

Thermostability of tropomyosins from the fast skeletal muscles of tropical fish species

Ming Chih Huang, Cheng Linn Lee, Yoshihiro Ochiai, Shugo Watabe

AGR - Biological Resource Sciences

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

In order to investigate the species-specific heat tolerance of tropical fishes, the thermodynamic properties of muscle tropomyosin, a member of myofibrillar proteins, were compared among milkfish, tilapia, grouper, and mudskipper. The purified tropomyosins were subjected to differential scanning calorimetry and circular dichroism spectrometry. To unveil the relationship between the stability and the amino acid sequences, the muscle tropomyosin genes of the four species were also cloned, and their deduced amino acid sequences were compared. Thermodynamic analysis revealed that the milkfish tropomyosin showed lower refolding ability after thermal denaturation, compared with those of the other species. The amino acid sequences of these tropomyosins were similar to each other, with the identity being in the range of 95–96%.

Original language	English
Pages (from-to)	1189-1202
Number of pages	14
Journal	Fish Physiology and Biochemistry
Volume	45
Issue number	3
DOIs	https://doi.org/10.1007/s10695-019-00632-7
Publication status	Published - 2019 Jun 15

Keywords

Amino acid sequence
Muscle tropomyosin
Thermostability
Tropical fish

ASJC Scopus subject areas

Biochemistry
Physiology
Aquatic Science

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abstract = "In order to investigate the species-specific heat tolerance of tropical fishes, the thermodynamic properties of muscle tropomyosin, a member of myofibrillar proteins, were compared among milkfish, tilapia, grouper, and mudskipper. The purified tropomyosins were subjected to differential scanning calorimetry and circular dichroism spectrometry. To unveil the relationship between the stability and the amino acid sequences, the muscle tropomyosin genes of the four species were also cloned, and their deduced amino acid sequences were compared. Thermodynamic analysis revealed that the milkfish tropomyosin showed lower refolding ability after thermal denaturation, compared with those of the other species. The amino acid sequences of these tropomyosins were similar to each other, with the identity being in the range of 95–96%.",

keywords = "Amino acid sequence, Muscle tropomyosin, Thermostability, Tropical fish",

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AU - Lee, Cheng Linn

AU - Ochiai, Yoshihiro

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PY - 2019/6/15

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