Differences in thermodynamic properties and 2D-PAGE behavior of fish skeletal muscle tropomyosins are likely due to a few amino acid replacements.
Subtle sequence variation may drive fish tropomyosin stability differences; leaves open relevance to human cardiac muscle protein research.
Tropomyosins were purified from the fast skeletal muscle of several fish species. While their behaviors on two-dimensional PAGE (2D-PAGE) were examined, their thermodynamic properties were compared by differential scanning calorimetry (DSC). Furthermore, full- and partial lengths of cDNAs encoding fast skeletal muscle tropomyosins were cloned from white croaker and walleye pollack, respectively, and their nucleotide and deduced amino acid sequences were determined. It was suggested that the differences observed in the above two analytical parameters among fish species were due to only a few amino acid replacements in the molecule.
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Ochiai et al. (2002) studied this question.
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