Tropomyosin was extracted with 1M potassium chloride solution from the dried muscle powder of carp and purified by isoelectric precipitation, ammonium sulfate fractionation and gel filtration using Sephadex G-200.
The ultraviolet spectrum of the carp tropomyosin showed the absence of a nucleotide contaminant. The absorbance for a 0.1% solution of 1cm path length at 278 mμ was 0.290. The viscometric properties of carp tropomyosin were similar to those of rabbit skeletal tropomyosin. Intrinsic viscosity of both tropomyosins was determined to be 0.36 dl/g. On SDS-polyacrylamide gel electrophoresis, carp tropo-myosin showed a single band with similar mobility to the faster one of two bands present in rabbit tropomyosin. Although tropomyosin inhibited the Mg2+-ATPase activity of desensitized carp actomyosin at 2mM Mg2+-ATP in the presence and absence of Ca2+, it had no effect on the Ca2+-sensitivity. In the presence of carp troponin, tropomyosin conferred Ca2+-sensitivity on the Mg2+-ATPase and super-precipitation of desensitized actomyosin.
It was suggested that the mechanisms and functions of the regulatory system in carp muscle were essentially the same as those of the rabbit.