魚類,ホタテガイ,ウサギ筋肉のミオシンとアクチンから合成したアクトミオシンの温度安定性
魚類,ホタテガイ,ウサギ筋肉のミオシンとアクチンから合成したアクトミオシンの温度安定性
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DOI：
10.2331/suisan.44.485
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发表时间：
1978-05
影响因子：
0.4
通讯作者：
敬子 山下;健一 新井;清義 西田
中科院分区：
文献类型：
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作者：
敬子 山下;健一 新井;清義 西田
肌球蛋白和肌动蛋白是从鱼背肌、兔骨骼肌和扇贝横纹收肌中制备的。肌动球蛋白是通过将肌球蛋白和肌动蛋白制剂以等重量比混合而以各种组合合成的。研究了合成肌动球蛋白的ATP敏感性和热稳定性。1.所有组合的肌球蛋白和肌动蛋白从鱼和兔的来源得到肌动球蛋白具有较高的ATP敏感性，而组合的扇贝肌球蛋白和肌动蛋白的鱼或扇贝产生肌动球蛋白具有较低的ATP敏感性。这些结果表明肌球蛋白和肌动蛋白的结合相对较弱。2.从Ca ~（2+）-ATP酶失活的一级速率常数（KD）判断，虽然人工肌动球蛋白的稳定性比肌球蛋白的稳定性高10倍左右，但含有一定肌球蛋白和各种肌动蛋白的人工肌动球蛋白对热变性的稳定性完全相同。3.在不同KCl浓度下，由鱼类和扇贝来源合成的肌动球蛋白的Ca ~（2+）-ATP酶的热失活速率常数几乎相同。
Myosin and actin were prepared from fish dorsal, rabbit skeletal, and scallop striated adductor muscles. Actomyosins were synthesized in various combinations of myosin and actin preparations by mixing them in an equal weight ratio. The ATP sensitivity and thermostability of the synthetic actomyosins were studied. 1. All combinations of myosin and actin from fish and rabbit sources gave actomyosins having a high ATP sensitivity, while the combinations of scallop myosin and actin of either fish or scallop produced actomyosins having a lower ATP sensitivity. These results suggest a relatively weak binding of myosin and actin. 2. Judging from the first order rate constant (KD) of inactivation of Ca2+-ATPase, it was found that synthetic actomyosins which contained a definite myosin with various actins maintained exactly the same stability against thermal denaturation, although the synthetic actomyosin is approximately 10 times more stable than its myosin moiety. 3. The thermal inactivation of Ca2+-ATPase of actomyosins synthesized from fish and scallop sources, assayed at various KCI concentrations, gave nearly the same rate constants.