ティラピア背筋のアクチンとミオシンの結合について

抄録

Actin and myosin were prepared separately from the dorsal muscle of tilapia (Tilapia mossambica) and actomyosin was reconstituted at various ratios of actin to myosin by weight.
It was found that the reconstitution of actomyosin restored the identical characteristics of natural actomyosin; that is, anomalous viscosity with respect to protein concentration and reversible dissociation into actin and myosin by ATP at high ionic strength, which resulted in high ATP-sensitivity, positive superprecipitation upon the addition of ATP at low ionic strength, and the enhancement of Mg₂₊ dependent ATPase activity.
These results support the conclusion that the biological activities of fish actin are essentially the same as those of rabbit.