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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Ochiai Y, Handa A, Watabe S, Hashimoto K

Laboratory of Marine Biochemistry, Faculty of Agriculture, University of Tokyo, Japan.

Int J Biochem. 1990;22(10):1097-103. doi: 10.1016/0020-711x(90)90107-e.

Fast skeletal myosin subfragment 1 (S1) was separated into two isozymes, S1(A1) and S1(A2), based on the associated alkali light chain, and their thermostabilities were compared. 2. Inactivation rate constants of Ca2(+)-ATPase (at 30 and 35 degrees C) were higher and heat-induced turbidity increase at 340 nm (at 40 degrees C) was faster with S1(A1) than with S1(A2), indicating a higher stability of S1(A2). 3. When S1 isozymes were incubated in the presence of excess alkali light chain, turbidity increase was markedly reduced, depending on the amount of light chain added. 4. Results obtained strongly suggest that alkali light chains are involved in the maintenance of myosin head structure.

快速骨骼肌肌球蛋白亚片段1（S1）根据相关的碱性轻链被分离为两种同工酶，即S1（A1）和S1（A2），并比较了它们的热稳定性。2. Ca2（+）-ATP酶的失活速率常数（在30和35摄氏度时），S1（A1）比S1（A2）更高，并且在340纳米处（40摄氏度时）热诱导的浊度增加，S1（A1）比S1（A2）更快，这表明S1（A2）具有更高的稳定性。3. 当S1同工酶在过量碱性轻链存在下孵育时，浊度增加明显减少，这取决于添加的轻链量。4. 所获得的结果强烈表明碱性轻链参与肌球蛋白头部结构的维持。

Ochiai Y, Handa A, Watabe S, Hashimoto K

Laboratory of Marine Biochemistry, Faculty of Agriculture, University of Tokyo, Japan.

Int J Biochem. 1990;22(10):1097-103. doi: 10.1016/0020-711x(90)90107-e.

Fast skeletal myosin subfragment 1 (S1) was separated into two isozymes, S1(A1) and S1(A2), based on the associated alkali light chain, and their thermostabilities were compared. 2. Inactivation rate constants of Ca2(+)-ATPase (at 30 and 35 degrees C) were higher and heat-induced turbidity increase at 340 nm (at 40 degrees C) was faster with S1(A1) than with S1(A2), indicating a higher stability of S1(A2). 3. When S1 isozymes were incubated in the presence of excess alkali light chain, turbidity increase was markedly reduced, depending on the amount of light chain added. 4. Results obtained strongly suggest that alkali light chains are involved in the maintenance of myosin head structure.

快速骨骼肌肌球蛋白亚片段1（S1）根据相关的碱性轻链被分离为两种同工酶，即S1（A1）和S1（A2），并比较了它们的热稳定性。2. Ca2（+）-ATP酶的失活速率常数（在30和35摄氏度时），S1（A1）比S1（A2）更高，并且在340纳米处（40摄氏度时）热诱导的浊度增加，S1（A1）比S1（A2）更快，这表明S1（A2）具有更高的稳定性。3. 当S1同工酶在过量碱性轻链存在下孵育时，浊度增加明显减少，这取决于添加的轻链量。4. 所获得的结果强烈表明碱性轻链参与肌球蛋白头部结构的维持。