Adenosine diphosphate effect on contractility of human muscle actomyosin: inhibition by ethanol and acetaldehyde.
Adenosine diphosphate effect on contractility of human muscle actomyosin: inhibition by ethanol and acetaldehyde.
复制标题
二磷酸腺苷对人肌肉肌动球蛋白收缩性的影响：乙醇和乙醛的抑制。
DOI：
10.1126/science.124949
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发表时间：
1975
期刊：
影响因子：
56.9
通讯作者：
E. Rubin
中科院分区：
文献类型：
--
作者：
S. Puszkin;E. Rubin
三磷酸腺苷镁(MG-2+-ATP)在体外可引起肌动蛋白和肌球蛋白的解离，而它的水解会导致肌球蛋白的重新解离。提纯的肌动蛋白与肌球蛋白在镁-2+-三磷酸腺苷存在下的相互作用可被微量的二磷酸腺苷(ADP)所刺激，二磷酸腺苷(ADP)是ATP水解的产物。相反，ADP可抑制肌动球蛋白复合体的解离。这些数据表明ADP起到调节肌肉收缩的作用。乙醇及其主要代谢物乙醛可抑制ADP的上述作用。当制剂中没有这些化合物时，这种抑制是可逆的。乙醇和乙醛对肌动球蛋白ADP反应的影响可能在酒精性肌病和心肌病的发病机制中起一定作用。
Magnesium adenosine triphosphate (Mg-2+-ATP) is known to produce dissociation of muscle actin and myosin in vitro, while its hydrolysis leads to reassociation. The interaction of purified actin and myosin from human muscle, in the presence of Mg-2+-ATP, was stimulated by minute amounts of adenosine diphosphate (ADP), a product of ATP hydrolysis. By contrast, the dissociation of the actomyosin complex was inhibited by ADP. These data suggest that ADP serves to modulate muscle contraction. Ethanol and its primary metabolite, acetaldehyde, inhibited these effects of ADP. The inhibition was reversible when the preparations were freed of these compounds. The effects of ethanol and acetaldehyde on the response of actomyosin to ADP may play a role in the pathogenesis of alcoholic myopathy and cardiomyopathy.