Henry S, Hobbs A
Department of Biochemistry, University of Western Australia, Nedlands, W.A., Australia 6907.
Insect Mol Biol. 1999 Aug;8(3):415-7. doi: 10.1046/j.1365-2583.1999.83125.x.
Several cDNA clones for a larval cuticular protein from Helicoverpa armigera were isolated and sequenced. The cDNA clones contain an open reading frame encoding a 109 residue protein which is homologous to other known cuticular proteins. The predicted protein appears to have a signal peptide which would be removed to give a mature protein of 91 amino acid residues with an Mr of 10 127. The mature protein, LCP1 (Larval Cuticular Protein), would be highly acidic, as is found for other cuticular proteins from flexible insect cuticles. The mRNA appears to be expressed throughout larval development although it is more highly expressed in the integument of the late final instar.
分离并测序了几个来自棉铃虫幼虫表皮蛋白的cDNA克隆。这些cDNA克隆包含一个开放阅读框,编码一种109个残基的蛋白质,该蛋白质与其他已知的表皮蛋白同源。预测的蛋白质似乎有一个信号肽,该信号肽会被去除,从而产生一个由91个氨基酸残基组成、分子量为10127的成熟蛋白质。成熟蛋白LCP1(幼虫表皮蛋白)将是高度酸性的,这与来自柔性昆虫表皮的其他表皮蛋白情况相同。尽管该mRNA在末龄后期的体壁中表达更高,但在整个幼虫发育过程中似乎都有表达。