Carvajal N, Martinez J, Fernandez M
Biochim Biophys Acta. 1977 Mar 15;481(1):177-83. doi: 10.1016/0005-2744(77)90149-8.
Human liver arginase (L-arginine amidinohydrolase, EC 3.5.3.1) was immobilised by attachment to nylon with glutaraldehyde as a crosslinking agent. Incubation of the immobilised tetrameric enzyme with EDTA followed by dialysis resulted in the dissociation of the enzyme into inactive matrix-bound and solubilised subunits. Both species recovered enzymatic activity after incubation with Mn2+, and the activity of the reactivated matrix-bound subunits was nearly 25% of that shown by the enzyme initially attached to the support in the tetrameric form. When the reactivated bound subunits were incubated with soluble subunits in the presence of Mn2+, they 'picked-up' from the solution an amount of protein and enzymatic activity almost identical to that initially lost by the immobilised tetramer after the dissociating treatment with EDTA. This occurred only in the presence of Mn2+. It is suggested that the reactivation of the subunits of arginase involves the initial formation of an active monomer, which then acquires a conformation that favours a reassociation to the tetrameric state.
人肝脏精氨酸酶（L-精氨酸脒基水解酶，EC 3.5.3.1）通过戊二醛作为交联剂附着在尼龙上进行固定化。将固定化的四聚体酶与EDTA一起孵育，然后透析，导致酶分解为无活性的与基质结合的亚基和可溶的亚基。两种产物在与Mn²⁺孵育后均恢复了酶活性，并且重新激活的与基质结合的亚基的活性接近最初以四聚体形式附着在载体上的酶所显示活性的25%。当重新激活的结合亚基在Mn²⁺存在下与可溶性亚基一起孵育时，它们从溶液中“摄取”了一定量的蛋白质和酶活性，几乎与固定化四聚体在经EDTA解离处理后最初损失的量相同。这仅在Mn²⁺存在时发生。有人提出，精氨酸酶亚基的重新激活涉及活性单体的初始形成，然后该单体获得有利于重新缔合为四聚体状态的构象。
