Tonks N K, Cohen P
Biochim Biophys Acta. 1983 Sep 14;747(1-2):191-3. doi: 10.1016/0167-4838(83)90140-1.
A Ca2+-dependent, calmodulin-stimulated protein phosphatase (EC 3.1.3.16) is known to be associated with calcineurin, a major calmodulin binding protein in brain. The protein phosphatase activity has now been shown to be retained by a substrate affinity column (thiophosphorylated myosin P-light chain Sepharose) in the presence of Ca2+, and to be eluted specifically with EGTA. Calcineurin behaved identically. This establishes that calcineurin is the Ca2+-dependent protein phosphatase, and that interaction of Ca2+ with the B-subunit is essential for substrate binding.
一种依赖钙离子、受钙调蛋白刺激的蛋白磷酸酶（EC 3.1.3.16）已知与钙调神经磷酸酶相关，钙调神经磷酸酶是大脑中一种主要的钙调蛋白结合蛋白。现已表明，在存在钙离子的情况下，该蛋白磷酸酶活性可被底物亲和柱（硫代磷酸化肌球蛋白轻链琼脂糖）保留，并能用乙二醇双四乙酸（EGTA）特异性洗脱。钙调神经磷酸酶表现相同。这证明钙调神经磷酸酶就是这种依赖钙离子的蛋白磷酸酶，并且钙离子与B亚基的相互作用对于底物结合至关重要。
