Flik G, Wendelaar Bonga S E, Fenwick J C
Comp Biochem Physiol B. 1983;76(4):745-54. doi: 10.1016/0305-0491(83)90388-7.
The characteristics of Ca2+-activated ATPase activities previously often postulated as components for the calcium transporting system in fish gills do not fulfil the requirements of a transport Ca2+-ATPase. The chelation of Ca2+- or Mg2+-ions is a prerequisite for the adenosinephosphate esters to serve as substrate for gill plasma membrane phosphatases. Ca2+-activated ATP hydrolysis results from the activity of a heterogeneous pool of phosphatases located in the plasma membranes of the branchial epithelium, as is concluded from substrate specificity tests and the effects of various inhibitors on these hydrolytic activities. In the present study only non-specific phosphatases could be shown.
先前常被假定为鱼类鳃中钙转运系统组成部分的钙离子激活的ATP酶活性特征，并不满足钙转运ATP酶的要求。钙离子或镁离子的螯合是磷酸腺苷酯作为鳃质膜磷酸酶底物的前提条件。钙离子激活的ATP水解是由位于鳃上皮质膜中的多种磷酸酶的活性引起的，这是根据底物特异性测试以及各种抑制剂对这些水解活性的影响得出的结论。在本研究中，仅显示出非特异性磷酸酶。
