Andersen S O
August Krogh Institute, Copenhagen University, Denmark.
Insect Biochem Mol Biol. 1998 May-Jun;28(5-6):421-34. doi: 10.1016/s0965-1748(98)00028-9.
Seven proteins from the abdominal cuticle of sexually mature locusts, Schistocerca gregaria, have been extracted, purified and sequenced. None of the proteins have been obtained from the pharate adult cuticle of the same species, and they probably represent post-ecdysially deposited endocuticular proteins. All the proteins contain the Rebers-Riddiford consensus sequence commonly found in cuticular proteins. The proteins are all N-terminally blocked by a pyroglutamine residue, and most of them contain one or more N-acetylhexosamine residues, presumably N-acetylgalactosamine (GalNAc), O-linked to either threonine or serine residues. One of the proteins is C-terminally blocked by an amide group. The unglycosylated forms of the proteins have molecular masses in the range from 9 to 20 kDa. The structures of the endocuticular proteins are discussed in relation to the special mechanical properties of locust abdominal cuticle.
已从成年性成熟的沙漠蝗（Schistocerca gregaria）腹部表皮中提取、纯化并测序了七种蛋白质。这些蛋白质均未从同一物种的蛹期成虫表皮中获得，它们可能代表蜕皮后沉积的内表皮蛋白。所有蛋白质都含有在表皮蛋白中常见的Rebers-Riddiford共有序列。这些蛋白质的N端均被焦谷氨酰胺残基封闭，并且大多数含有一个或多个N-乙酰己糖胺残基，推测为N-乙酰半乳糖胺（GalNAc），通过O-连接与苏氨酸或丝氨酸残基相连。其中一种蛋白质的C端被酰胺基团封闭。这些蛋白质的未糖基化形式的分子量在9至20 kDa范围内。结合蝗虫腹部表皮的特殊力学特性，对内表皮蛋白的结构进行了讨论。
