Abstract
Myosin, reconstituted actomyosin and myofibril were prepared from the requiem shark Triakis scyllia, and their urea-resistibilities were measured at 25°C, taking Ca2+-ATPase activity as a parameter.In the absence of urea, both the reconstituted actomyosin and myofibril showed about 10 times as high a resistibility as myosin, the magnitude which was clearly less than that with the carp, 18-20 times.In 1.4 M urea, on the other hand, the reconstituted actomyosin and myofibril exhibited a higher resistibility than myosin. The magnitude was 4-6 times with requiem shark, in contrast to less than 2 times with carp, suggesting a species-specificity of requiem shark myofibrillar proteins.
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