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飞蝗(Locusta migratoria)表皮蛋白的分离、特性鉴定及N端序列研究

Isolation, characterization, and N-terminal sequence studies of cuticular proteins from the migratory locust, Locusta migratoria.

作者信息

Højrup P, Andersen S O, Roepstorff P

出版信息

Eur J Biochem. 1986 Jan 2;154(1):153-9. doi: 10.1111/j.1432-1033.1986.tb09371.x.

DOI:10.1111/j.1432-1033.1986.tb09371.x
PMID:3943519
Abstract

The cuticle of the migratory locust, Locusta migratoria, contains more than a hundred different structural proteins, which can be extracted before but not after the cuticle is sclerotized. Fourteen of the proteins have been purified, covering a pI range of 6.4-10.6 and a molecular mass range of 15.2-36.8 kDa. The amino acid sequence from the N-terminal, ranging in length over 10-59 residues, have been obtained for eight of the proteins. A number of similarities, both in amino acid composition and in sequences, indicate that the proteins belong to a new protein family, characterized by an N-terminal part which is rich either in glycine, tyrosine and leucine or in hydrophilic amino acids, followed by a very alanine-rich portion. Similarities between this family of proteins and other structural proteins from insects are discussed.

摘要

飞蝗(Locusta migratoria)的表皮含有一百多种不同的结构蛋白,这些蛋白可在表皮硬化之前而非之后提取。其中14种蛋白质已被纯化,其等电点范围为6.4 - 10.6,分子量范围为15.2 - 36.8 kDa。已获得其中8种蛋白质N端长度在10 - 59个残基范围内的氨基酸序列。氨基酸组成和序列上的一些相似性表明,这些蛋白质属于一个新的蛋白质家族,其特征是N端部分富含甘氨酸、酪氨酸和亮氨酸或亲水性氨基酸,随后是一个非常富含丙氨酸的部分。本文还讨论了该蛋白质家族与昆虫其他结构蛋白之间的相似性。

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