Scutari G, Ballestrin G, Branca D, Boninsegna A
Boll Soc Ital Biol Sper. 1983 Oct 30;59(10):1391-7.
Treatment of erythrocyte membrane fragments with the amino group reagent sodium trinitrobenzenesulphonate (TNBS) leads to significant alteration of the kinetic properties of the membrane-bound (Ca2+ + Mg2+) and Mg2+-dependent ATPases, which appear to increase their affinity towards divalent cations and to decrease their maximal rates. Although it has not been possible to ascertain whether the amino groups involved in the TNBS effect belong to the membrane phospholipids or to the ATPase proteins, it appears that such groups play an essential role in the hydrolytic activity of the divalent cation-dependent ATPases, either by affecting the enzymes' microenvironment or by being directly involved in the enzymes'catalytic mechanism.
用氨基试剂三硝基苯磺酸钠（TNBS）处理红细胞膜片段，会导致膜结合的（Ca2+ + Mg2+）依赖性ATP酶和Mg2+依赖性ATP酶的动力学特性发生显著改变，这些酶似乎增加了对二价阳离子的亲和力，并降低了其最大反应速率。尽管尚无法确定参与TNBS效应的氨基是属于膜磷脂还是ATP酶蛋白，但这些基团似乎在二价阳离子依赖性ATP酶的水解活性中起着至关重要的作用，要么通过影响酶的微环境，要么直接参与酶的催化机制。
