Norup T, Berg T, Stenholm H, Andersen S O, Højrup P
Department of Molecular Biology, Odense University, Denmark.
Insect Biochem Mol Biol. 1996 Sep-Oct;26(8-9):907-15. doi: 10.1016/s0965-1748(96)00052-5.
Urea-extractable proteins have been purified from the cephalothoracic cuticle of mature Araneus diadematus spiders. Two-dimensional gel electrophoresis showed at least 12 major proteins, with pIs between 4.5 and 8.5. Five proteins were purified and their primary structure determined, using a combination of mass spectrometry and Edman degradation. Based on the amino acid sequence the proteins can be divided into two groups, both characterized by hydrophobic regions dominated by Ala, Pro and Val. Sequence similarity was observed between all the spider cuticle proteins and a number of proteins from other arthropod cuticles. Although the similarity seemed to be confined only to a region in the central part of the molecules, it does link these very distantly related species.
已从成年十字园蛛的头胸部角质层中纯化出尿素可提取蛋白。二维凝胶电泳显示至少有12种主要蛋白质，其等电点在4.5至8.5之间。利用质谱和埃德曼降解相结合的方法纯化了5种蛋白质并确定了其一级结构。根据氨基酸序列，这些蛋白质可分为两组，其特征均为以丙氨酸、脯氨酸和缬氨酸为主的疏水区域。在所有蜘蛛角质层蛋白与许多其他节肢动物角质层蛋白之间观察到了序列相似性。尽管这种相似性似乎仅局限于分子中部的一个区域，但它确实将这些亲缘关系非常远的物种联系了起来。
