Yamamoto K
Department of Bioengineering, Soka University, Tokyo.
J Biochem. 1993 Dec;114(6):770-2. doi: 10.1093/oxfordjournals.jbchem.a124254.
We describe cross-linking conditions for myosin subfragment-1 and actin with 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide, with which the compositions of cross-linked species can be altered. The specific Mg-ATPase activity of cross-linked subfragment-1 in these preparations was almost the same in spite of the differences in the compositions of the cross-linked species. This suggests that the two kinds of cross-linked species have almost the same ATPase activity, and that the cross-linking at these different sites nearly equally facilitates the formation of the strong binding state which accompanies the release of ADP and Pi.
我们描述了用1-乙基-3-[3-(二甲氨基)丙基]碳二亚胺对肌球蛋白亚片段-1和肌动蛋白进行交联的条件，利用该条件可改变交联产物的组成。尽管交联产物的组成存在差异，但这些制剂中交联亚片段-1的比Mg-ATP酶活性几乎相同。这表明这两种交联产物具有几乎相同的ATP酶活性，并且在这些不同位点的交联几乎同等程度地促进了伴随ADP和Pi释放的强结合状态的形成。
