Studies on Thermal Denaturation of Fish Myoglobins using Differential Scanning Calorimetry, Circular Dichroism, and Tryptophan Fluorescence

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  • Chanthai Saksit
    Department of Chemistry, Faculty of Science and Technology, Sophia University
  • Ogawa Masahiro
    Department of Chemistry, Faculty of Science and Technology, Sophia University
  • Tamiya Toru
    Department of Chemistry, Faculty of Science and Technology, Sophia University
  • Tsuchiya Takahide
    Department of Chemistry, Faculty of Science and Technology, Sophia University

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  • Studies on Thermal Denaturation of Fish

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Myoglobins from yellowfin tuna, bonito and yellowtail exhibited two distinct endothermic peaks reflecting multiple states of structural unfolding, whereas those of sheep and sperm whale myoglobins followed a two-state process. This indicated that the thermal unfolding of fish myoglobins is predominantly a multi-state process differing from that of the mammalian ones. Changes in dependence on temperature of an α-helix content and a tryptophan fluorescence intensity were found to be decreased more for fish myoglobins compared with those of the mammalian myoglobins. Consequently, fish myoglobins showed a lower recovery of the α-helix and tertiary structure than that of the mammalian proteins. These results are thermally attributed to low conformational stability of the fish proteins. Therefore, fish myoglobins exhibit a rather labile structural folding, suggesting a greater susceptibility to heat denaturation than that of the mammalian myoglobins.

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