Kuczmarski E R, Pagone J
J Muscle Res Cell Motil. 1986 Dec;7(6):510-6. doi: 10.1007/BF01753567.
Using native myosin phosphorylated on either the heavy chain or the light chain, we have isolated myosin phosphatases from extracts of vegetative Dictyostelium amoeba. Two phosphatases were resolved by DEAE-cellulose chromatography. One of these phosphatases removed phosphate from heavy chain or light chain at approximately the same rate. The other phosphatase appeared to be much more specific for phosphorylated myosin heavy chain. Although these enzymes removed phosphate from other phosphoprotein substrates such as histone or casein, they did so at a much lower rate. Both enzymes required magnesium for activity, but appeared to be independent of calcium.
利用在重链或轻链上磷酸化的天然肌球蛋白，我们从营养期盘基网柄菌变形虫的提取物中分离出了肌球蛋白磷酸酶。通过DEAE - 纤维素色谱法分离出了两种磷酸酶。其中一种磷酸酶以大致相同的速率从重链或轻链上去除磷酸基团。另一种磷酸酶似乎对磷酸化的肌球蛋白重链具有更高的特异性。尽管这些酶能从其他磷蛋白底物如组蛋白或酪蛋白上去除磷酸基团，但速率要低得多。两种酶的活性都需要镁，但似乎与钙无关。
