Amino acid sequence studies on endocuticular proteins from the desert locust, Schistocerca gregaria
Amino acid sequence studies on endocuticular proteins from the desert locust, Schistocerca gregaria
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DOI：
10.1016/s0965-1748(98)00028-9
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发表时间：
1998-05-01
影响因子：
3.8
通讯作者：
Andersen, SO
中科院分区：
文献类型：
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作者：
Andersen, SO
从性成熟蝗虫Schistocerca gregaria的腹部角质层中提取了7种蛋白质，并进行了纯化和测序。没有一种蛋白质是从同一物种的pharate成体角质层中获得的，它们可能代表蜕皮后沉积的表皮内蛋白质。所有的蛋白质都含有表皮蛋白中常见的Rebers-Riddiford共有序列。这些蛋白质的N-末端都被焦谷氨酰胺残基封闭，并且它们中的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），O-连接到苏氨酸或丝氨酸残基。其中一种蛋白质的C-末端被酰胺基团封闭。蛋白质的非糖基化形式具有9至20 kDa的分子量。本文还讨论了蝗虫腹部表皮内蛋白质的结构与其特殊力学性质的关系。(C)1998爱思唯尔科技有限公司。保留所有权利。
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. (C) 1998 Elsevier Science Ltd. All rights reserved.