Abstract
Thermal denaturation of fish myosins was studied by turbidity measurements, differential scanning calorimetry (DSC), circular dichroism (CD), intrinsic fluorescence and 8-anilino-1-naphthalene sulfonic acid binding studies. Results of DSC and turbidity studies showed that thermal aggregation of myosins from three fish species (cod, herring and silver hake) proceeded prior to the final stage of denaturation of the myosin molecules. CD and fluorescence measurements revealed that all fish myosins exhibited similar helix melting profiles, but the unfolded domains of each fish species displayed different surface hydrophobicities. Over a temperature range of 30–50°C, greater hydrophobic surface area was exposed by cod and silver hake myosins than by herring. The extent of myosin aggregation was species dependent; cod > silver hake > herring. Therefore, exposure of hydrophobic domain(s) is a prerequisite for the formation of large myosin aggregates. The effect of the sequence of unfolding of fish myosin molecules on thermal aggregation is discussed.
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