Wagner P D, Yount R H
J Biol Chem. 1976 Sep 10;251(17):5424-6.
Heavy meromyosin treated with the ATP analog, 6,6'-dithiobis(inosinyl-5'-yl imidodiphosphate), (slppNHp)2, in the presence of adenyl-5'-yl imidodiphosphate at 0 degrees loses its EDTA-ATPase activity and actin binding ability in a parallel manner. Studies with myosin show that under the above conditions (slppNHp)2 reacts preferentially with the single cysteines of the alkali light chains (Mr = 20,700 and 16,500) suggesting a role for these subunits in regulating actin-myosin interaction and ATP cleavage.
在0℃下，重酶解肌球蛋白在腺苷-5'-基咪唑二磷酸存在的情况下，用ATP类似物6,6'-二硫代双（肌苷-5'-基亚氨基二磷酸）[（slppNHp）2]处理后，其EDTA-ATP酶活性和肌动蛋白结合能力会以平行的方式丧失。对肌球蛋白的研究表明，在上述条件下，（slppNHp）2优先与碱性轻链（分子量分别为20700和16500）的单个半胱氨酸发生反应，这表明这些亚基在调节肌动蛋白-肌球蛋白相互作用和ATP裂解中发挥作用。
