Hagiwara H, Hasebe H, Yamazaki S, Tamaura Y, Inada Y
Experientia. 1979 Dec 15;35(12):1558-9. doi: 10.1007/BF01953190.
The enzymic activity of Mg2+- or Ca2+-stimulated ATPase from Escherichia coli was inhibited by one of the troponin components, TN-I, and by mitochondrial ATPase inhibitor (F1-inhibitor). The inhibitory ability of component TN-I against Mg2+-stimulated AtPase activity was lost after digestion of component TN-I with trypsin. The Mg2+-stimulated ATPase activity inhibited by component TN-I was completely restored by the addition of another troponin component TN-C.
来自大肠杆菌的Mg2+或Ca2+刺激的ATP酶的酶活性受到肌钙蛋白组分之一TN-I以及线粒体ATP酶抑制剂(F1抑制剂)的抑制。用胰蛋白酶消化TN-I组分后,TN-I组分对Mg2+刺激的ATP酶活性的抑制能力丧失。被TN-I组分抑制的Mg2+刺激的ATP酶活性通过添加另一种肌钙蛋白组分TN-C而完全恢复。