Hakim G, Itano T, Verma A K, Penniston J T
Biochem J. 1982 Nov 1;207(2):225-31. doi: 10.1042/bj2070225.
A Ca2+-ATPase (Ca2+- and Mg2+-requiring ATPase) was purified from a synaptic plasma-membrane fraction of rat brain. This enzyme had properties similar to those of plasma-membrane Ca2+-ATPases from other organs: its splitting of ATP was dependent on both Ca2+ and Mg2+, it bound in a Ca2+-dependent fashion to calmodulin-Sepharose and it cross-reacted with specific antibodies raised against human erythrocyte-membrane Ca2+-ATPase. It had an apparent Mr of 138 000, similar to those of plasma-membrane ATPases from human erythrocyte and from dog heart sarcolemma. Previous high-Ca2+-affinity ATPases observed in brain had Mr 100 000; in at least one case, such an ATPase probably represented a different type of enzyme, derived from coated vesicles.
从大鼠脑突触质膜组分中纯化出一种钙 - ATP酶(需要钙和镁的ATP酶)。这种酶具有与其他器官质膜钙 - ATP酶相似的特性:其ATP水解依赖于钙和镁,它以钙依赖的方式与钙调蛋白 - 琼脂糖结合,并且能与针对人红细胞膜钙 - ATP酶产生的特异性抗体发生交叉反应。它的表观分子量为138000,与人红细胞和犬心肌肌膜的质膜ATP酶相似。先前在脑中观察到的高钙亲和力ATP酶分子量为100000;至少在一个案例中,这种ATP酶可能代表一种不同类型的酶,源自被膜小泡。