Abstract
Effect of pyrophosphate (PP) on the dissociation and stability of natural actomyosin (NAM) from kuruma prawn muscle was studied in comparison with adenosine 5′-triphosphate (ATP). In the presence of PP up to 5 mM, NAM exhibited lower Mg 2+-ATPase activity ( P < 0.05), while no marked change was observed in NAM treated with ATP at all concentrations tested (0.25–10 mM) ( P > 0.05). Ca 2+-ATPase activity of NAM treated with 5 mM PP decreased markedly when incubated at temperatures greater than 30 °C, suggesting lowered thermal stability of the liberated myosin molecule. Nevertheless, Ca 2+-ATPase activity of ATP-treated NAM was similar to the control NAM. In the presence of 5–10 mM MgCl 2, NAM treated with 5 mM PP underwent dissociation effectively, as evidenced by a greater decrease in Mg 2+-ATPase activity as well as an increased band intensity of actin released. Therefore, addition of PP in combination with MgCl 2 was more effective than was ATP in dissociating the actomyosin complex of prawn muscle.
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