Interactions of dicyclohexylcarbodiimide with myelin proteolipid.
Interactions of dicyclohexylcarbodiimide with myelin proteolipid.
复制标题
二环己基碳二亚胺与髓磷脂蛋白脂质的相互作用。
DOI：
10.1073/pnas.79.3.941
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发表时间：
1982
影响因子：
11.1
通讯作者：
Lees,MB
中科院分区：
文献类型：
--
作者：
Lin,LF;Lees,MB
已知二环己基碳二亚胺(DCD)优先与质子转运系统的蛋白脂亚单位结合，从而抑制质子转运。在本研究中，我们发现，在水介质中，DCD与中枢神经系统髓鞘的主要蛋白质--牛白质蛋白脂脱脂蛋白结合。结合依赖于时间、温度和浓度，并且不被亲水性碳二亚胺1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide.抑制相反，当孵育在氯仿/甲醇中进行时，DCD没有明显的标记。在分离的大鼠髓鞘中，DCCD特异性地与蛋白脂结合，而不与髓鞘碱性蛋白结合。用9-氨基吖啶荧光猝灭法检测与髓鞘蛋白脂脱辅基蛋白重组的脂质体转运质子。含蛋白脂脂的脂质体与DCD预先孵育后，转运受到抑制。这些研究对髓鞘蛋白脂可能的离子传递功能和髓鞘内运输过程的发生具有重要的意义。
Dicyclohexylcarbodiimide (DCCD) is known to bind preferentially to a proteolipid subunit of proton-translocating systems and thereby to inhibit proton transport. In the present study we show that, in an aqueous medium, DCCD binds to the bovine white matter proteolipid apoprotein, the major protein of central nervous system myelin. The binding is dependent on time, temperature, and concentration and is not inhibited by the hydrophilic carbodiimide 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide. By contrast, when the incubation is carried out in chloroform/methanol no labeling by DCCD is demonstrable. In isolated rat myelin, DCCD binds specifically to the proteolipid and not to the myelin basic proteins. Liposomes reconstituted with the myelin proteolipid apoprotein transport protons, as assayed by quenching of the fluorescence of 9-aminoacridine. Preincubation of proteolipid-containing liposomes with DCCD results in an inhibition of transport. These studies have important implications for a possible ionophoric function of the myelin proteolipid and for the occurrence of transport processes within myelin.