CAJ | 학술논문

以生物素标记的钙调素为探针，筛选拟南芥λZAPⅡ表达文库，分离得到9个阳性克隆。融合蛋白的Westem印迹分析表明，这些阳性克隆确是编码钙调素结合蛋白的(图2，3)，并且其中Y9等8个克隆编码的融合蛋白与钙调素有依赖于钙离子的结合(图3B)；而唯独Y7编码的融合蛋白与钙调素的结合，与CaMBP-10一样，不依赖于钙离子的存在(图3A)。
이생물소표기적개조소위탐침，사선의남개λZAPⅡ표체문고，분리득도9개양성극륭。융합단백적Westem인적분석표명，저사양성극륭학시편마개조소결합단백적(도2，3)，병차기중Y9등8개극륭편마적융합단백여개조소유의뢰우개리자적결합(도3B)；이유독Y7편마적융합단백여개조소적결합，여CaMBP-10일양，불의뢰우개리자적존재(도3A)。
Using protein-protein interaction,an Arabidopsis λZAP Ⅱ cDNAexpression library was screened with biotinylated calmodulin as a probe. Nine positive clones were isolated.The results of Western blotting of fusion proteins indicated that all these positive clones could synthesize peptides which could bind calmodulin ( Figs. 2,3). Eight of them bound calmodulin depending on the presence of Ca2+( Fig. 3 B), but only one fusion protein encoded by Y7 cDNA clone, which was the same as CaM BP-10, could bind CaM in a way independent of Ca2+ ( Fig. 3A).