ウサギ骨格筋とティラピア背筋のミオシンおよびアクトミオシン Ca2+-ATPase の温度安定性について

概要

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1) The ATP-sensitivities of the myosin and actomyosin preparations employed in this report were found to be 2 for rabbit myosin, 3 for tilapia myosin, 117 for rabbit actomyosin, and 105 for tilapia actommyosin, respectively. 2) The thermal inactivation of Ca2+-ATPase in 0.6 M KC1 at pH 6.8 was studied. The inactivation consisted of a single first order reaction with either myosin or actomyosin alone, whereas it consisted of two first order reactions with mixtures of myuosin plus actomyosin. 3) The inactivation rate was 27.8×10-5 sec-1 for rabbit myosin, 0.41×10-5 sec-1 for rabbit actomyosin, 67.1×10-5 sec-1 for tilapia myosin, and 1.80×10-5 sec-1 for tilapia actomyosin, respectively. 4) The inactivation rate obtained with the moyosin plus actomyosin mixtures were 12.5×10-5 sec-1 and 0.83×10-5sec-1 for rabbit preparations, and 16.0×10-5 sec-1 and 2.50×10-5 sec-1 for tilapia preparations. Based on the results described above, a method is suggested for testing the extracts of rabbit and fish muscles for actin and myosin content.