用乙二醇替代水对肌球蛋白与肌动蛋白及5'-腺苷酰亚胺二磷酸之间相互作用的修饰
Modification of the interactions of myosin with actin and 5'-adenylyl imidodiphosphate by substitution of ethylene glycol for water.
作者信息
Marston S B, Tregear R T
出版信息
Biochem J. 1984 Jan 1;217(1):169-77. doi: 10.1042/bj2170169.
Abstract
We studied the effect of replacing water by ethylene glycol as solvent on the properties of skeletal muscle myosin, myosin subfragment-1 (S1) and heavy meromyosin. Ethylene glycol (50%, v/v) had no detectable effect on the affinity of myosin or actomyosin for the substrate analogue 5'-adenylyl imidodiphosphate (AMPPNP). However, the rate constants for formation and dissociation of the myosin X MgAMPPNP complex were reduced 200-fold; the logarithm of the dissociation rate was roughly proportional to the fractional concentration of ethylene glycol. Nucleotide dissociation was accelerated at least 300-fold by pure actin but remained slow with regulated actin in the absence of Ca2+. Ethylene glycol substitution reduced the affinity of S1 and the S1 X MgAMPPNP complex for actin equally (100-fold at 50% ethylene glycol). These results show that ethylene glycol has specific effects on myosin's enzymic mechanism, which can account for its effect on the tension and stiffness of glycerinated muscle fibres.
摘要
我们研究了用乙二醇替代水作为溶剂对骨骼肌肌球蛋白、肌球蛋白亚片段-1（S1）和重酶解肌球蛋白性质的影响。乙二醇（50%，v/v）对肌球蛋白或肌动球蛋白与底物类似物5'-腺苷酰亚胺二磷酸（AMPPNP）的亲和力没有可检测到的影响。然而，肌球蛋白与MgAMPPNP复合物形成和解离的速率常数降低了200倍；解离速率的对数与乙二醇的分数浓度大致成比例。在纯肌动蛋白存在下，核苷酸解离加速了至少300倍，但在没有Ca2+的情况下，调节型肌动蛋白存在时核苷酸解离仍然缓慢。乙二醇替代同样降低了S1以及S1与MgAMPPNP复合物对肌动蛋白的亲和力（在50%乙二醇时降低100倍）。这些结果表明，乙二醇对肌球蛋白的酶促机制有特定影响，这可以解释其对甘油化肌纤维张力和刚度的影响。
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