Andreasen L, Højrup P, Andersen S O, Roepstorff P
Department of Molecular Biology, Odense University, Denmark.
Eur J Biochem. 1993 Oct 1;217(1):267-73. doi: 10.1111/j.1432-1033.1993.tb18242.x.
The primary structures of two basic low-molecular-mass proteins, Lm-67 and Lm-70 from the pharate cuticle of the migratory locust, Locusta migratoria, were determined. The sequencing strategy was based on combined use of plasma--desorption mass spectrometry (PDMS) and automatic Edman degradation of the proteins and their enzymically derived peptides. The mass-spectral data showed the presence of two proteins in each preparation. For protein preparation Lm-67, this was indicated by the mass spectrum of the intact protein. For protein preparation Lm-70, the presence of two variants only became evident by mass-spectrometric analysis of the enzymically derived peptides. Both proteins show strong similarity to other exocuticular proteins from L. migratoria.
测定了来自飞蝗(Locusta migratoria)羽化前表皮的两种碱性低分子量蛋白质Lm - 67和Lm - 70的一级结构。测序策略基于等离子体解吸质谱(PDMS)与蛋白质及其酶解衍生肽段的自动埃德曼降解相结合的方法。质谱数据显示每种制剂中存在两种蛋白质。对于蛋白质制剂Lm - 67,完整蛋白质的质谱表明了这一点。对于蛋白质制剂Lm - 70,只有通过对酶解衍生肽段的质谱分析,两种变体的存在才变得明显。这两种蛋白质与飞蝗的其他外表皮蛋白具有很强的相似性。