Abstract
Some biochemical properties of the Mr 52,000 component of Akazara scallop striated adductor troponin, which had been tentatively identified as troponin-I, were compared with those of rabbit troponin-I. Both the Mr 52,000 component and rabbit troponin-I together with rabbit tropomyosin inhibited the Mg-ATPase activity of rabbit reconstituted actomyosin to 1/10 of the original activity. The inhibition was neutralized by the addition of Akazara scallop and rabbit troponin-C or Patinopecten scallop calmodulin. The Mr 52,000 component and rabbit troponin-I were insoluble below 0.15 M KCl, but were solubilized by complexing with an equimolar amount of troponin-C or calmodulin. On alkaline urea-polyacrylamide gel electrophoresis, the Mr 52,000 component as well as rabbit troponin-I was found to form a stable complex with troponin-C or calmodulin in the presence of Ca2+.
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