牵牛花粉表面蛋白SDS-PAGE分析  

Surface Proteins Analyzed by SDS-PAGE in the Pharbitis nil(Linn.) Choisy Pollen

作　　者：李叶峰[1] 谢慧慧[1] 刘晓红[1] 王群[1] 陆小平[1] 

机构地区：[1]苏州大学金螳螂建筑与城市环境学院,江苏苏州215123

出　　处：《河南农业科学》2010年第1期99-102,共4页Journal of Henan Agricultural Sciences

摘　　要：花粉表面蛋白在植物自交亲和反应中起着重要作用。为了探讨植物自交亲和性分子机制,以裂牵牛的花粉和柱头为材料,对其花粉表面蛋白和柱头表面蛋白进行了SDS-PAGE分析,通过对比不同的提取方式获得的花粉表面蛋白的电泳谱带,获得了最佳的样品提取方法。通过分析花粉和柱头表面蛋白的电泳波谱发现,花粉表面蛋白和柱头表面蛋白的电泳谱带中有2条共同的蛋白带,推断这2条谱带可能与花粉的识别反应有关。为了证明SDS-PAGE电泳获得的信息是来自花粉表面的蛋白,而不是来自花粉吸水涨裂后花粉原生质蛋白,对水浸提后的牵牛花粉粒进行显微镜观察,发现很少有破裂的花粉粒,进一步确定了传粉受精过程中是花粉表面蛋白与雌蕊组织间的识别反应。Pharbitis nil （Linn.） Choisy were selected to be materials whose pollen surface proteins and stigma proteins were analyzed by SDS-PAGE to research its self-incompatibility mecha nism. By analyzing the pollen and the stigma surface proteinelectrophoretic spectrum, two common protein stripes were found. It was deduced that the two common protein bands were relaled to self-incompatibility. In order to prove the etectrophoretic spectrum information obtained from the pollen surface protein, the pollens extracted by water extraetion method were observed using microscope. The result showed that very few pollen grains ruptured. So, the process of pollination fertilization shoud be the response of pollen surface protein to the pistil. Furthermore, the best method was obtained by comparing the electrophoretic spectrum stripe of surface protein extracted by different methods.

关 键 词：裂叶牵牛 花粉表面蛋白 SDS-PAGE电泳 

分 类 号：S681.6[农业科学—观赏园艺]