自豬腦皮質(porcine brain cortex)中純化出的後突觸質密區(postsynaptic density, 簡稱PSD)為一個大型的蛋白質複合體(protein complex)，其內包含了數百種的蛋白質。為了研究像這樣的大型蛋白質複合體內部的蛋白質間交互作用，我們發展了一套方法，在打散PSD的整體結構之餘，還能夠維持部分其原有的局部蛋白質交互作用。利用這樣的PSD樣本以及免疫吸附(immunoabsorption)，我們發現PSD-95會與α-, β-subunits of calcium, calmodulin-dependent protein kinase II (CaMKIIα及CaMKIIβ), α-tubulin, β-tubulins, NMDA receptors及Chapsyn-110一起被分離出來，而CaMKIIα則會與α-tubulin、β-tubulin、CaMKIIβ及少量的PSD-95一起被分離出來。將PSD以可切裂的交聯反應劑處理，再將其打散，進行免疫吸附，以對角線電泳(diagonal electrophoresis)分析，則進一步發現α-tubulin與CaMKIIα有直接的交互作用關係。這些結果指示出CaMKIIα、α-tubulin、β-tubulin、CaMKIIβ會在PSD中形成一個次級蛋白質複合體(protein subcomplex)，這個蛋白質複合體會在PSD中形成一個核心構造，與其他PSD中的蛋白質，如PSD-95或Chapsyn-110，形成直間或間接的交互作用，組織PSD的整體結構。這份研究同時也指示了一套可用於研究大型複雜蛋白質複合體中的蛋白質間交互作用的方法。

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