Jespersen S, Højrup P, Andersen S O, Roepstorff P
August Krogh Institute, Copenhagen O, Denmark.
Comp Biochem Physiol B Biochem Mol Biol. 1994 Sep;109(1):125-38. doi: 10.1016/0305-0491(94)90149-x.
The complete primary structures of two variants of a protein, Abd-5, isolated from the endocuticles of the migratory locust Locusta migratoria and the desert locust Schistocerca gregaria, have been determined. The proteins from the two species are N-terminally blocked with pyroglutamic acid. Their sequences differed only in two positions. Comparison of the sequences to those of other cuticular proteins shows that moderate homologies exist to 11 other cuticular proteins from insects representing four different orders. Amino acid residues in certain positions appear to be strictly conserved.
已确定从飞蝗Locusta migratoria和沙漠蝗Schistocerca gregaria的内表皮中分离出的一种蛋白质Abd-5的两种变体的完整一级结构。这两个物种的蛋白质在N端被焦谷氨酸封闭。它们的序列仅在两个位置不同。将这些序列与其他表皮蛋白的序列进行比较表明，与代表四个不同目的昆虫的其他11种表皮蛋白存在适度的同源性。某些位置的氨基酸残基似乎严格保守。
