Dzhandzhugazyan K, Bock E
Protein Laboratory, University of Copenhagen, Panum Institute, Denmark.
FEBS Lett. 1993 Dec 27;336(2):279-83. doi: 10.1016/0014-5793(93)80820-k.
In this study a possible association between (Ca(2+)-Mg2+)-ATPase activity and the neural cell adhesion molecule, NCAM, was investigated. The effects of various detergents on ATPase activity were evaluated, and it was found that solubilization of rat brain microsomes with 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate, CHAPS, released a major fraction of the (Ca(2+)-Mg2+)-ATPase activity together with NCAM. Using different types of solid phase immunoadsorption it was shown that NCAM antibodies selectively isolated ATPase activity. Furthermore, agarose gel immunoelectrophoresis of solubilized brain microsomes followed by ATPase assay directly in the gel revealed ATPase activity associated with the NCAM immunoprecipitate. The NCAM-associated enzyme activity had a broad nucleoside triphosphate specificity and no strict selectivity for divalent cations, indicating that the enzyme probably is an ecto-ATPase. This raises a series of intriguing questions in relation to NCAM adhesive functions.
在本研究中，对（Ca(2+)-Mg2+）-ATP酶活性与神经细胞黏附分子NCAM之间可能存在的关联进行了调查。评估了各种去污剂对ATP酶活性的影响，发现用3-[(3-胆酰胺丙基)二甲基铵]-1-丙烷磺酸盐（CHAPS）溶解大鼠脑微粒体时，释放出大部分（Ca(2+)-Mg2+）-ATP酶活性以及NCAM。使用不同类型的固相免疫吸附表明，NCAM抗体可选择性分离ATP酶活性。此外，对溶解的脑微粒体进行琼脂糖凝胶免疫电泳，随后直接在凝胶中进行ATP酶测定，结果显示ATP酶活性与NCAM免疫沉淀物相关。与NCAM相关的酶活性对核苷三磷酸具有广泛的特异性，对二价阳离子没有严格的选择性，这表明该酶可能是一种胞外ATP酶。这就引发了一系列与NCAM黏附功能相关的有趣问题。
