잉어의 배육 골격근에서 actomyosin을 추출하여 몇 가지 생물물리화학적인 성질을 측정 검토한 결과는 다음과 같다. 즉, actamyosin의 침강 정수($s_{20},;_omega$)는 24.76s이고 그 점성은 단백 농도의 증가와 더불어 급상승하여 다른 actomyosin의 그것과 비숫한 경향을 보였다. 그리고, ATP-sensitivity는 $147~176$이었고, PH영향하에서 ATPase activity는 산성측이 6,0부근, 알칼리성측이 9.5부근이었으므로 ATPase activating site가 산, 알칼리 양측에 있음을 알았다.
Natural actomyosin was extracted from the dorsal muscle of carp (Cyprinus carpio), and some Physico-chemical properties were determined. The sedimentation constant ($s_{20},;_omega$) of the purified skeletal muscle actomyosin was about 24.76s and the ATP sensitivity 147-176. The specific viscosity was rapidly ascended with the increase of protein concentration as other vertebrate actomyosins. ATPase activating site under the effect of pH variation was showed on the both sides of acid and base resembling with the tendency of rabbit skeletal muscle actomyosin, and found at 6.0 on the acidic side and at 9.5 on the basic side.
