THE PRIMARY STRUCTURE OF AN ENDOCUTICULAR PROTEIN FROM 2 LOCUST SPECIES, LOCUSTA-MIGRATORIA AND SCHISTOCERCA-GREGARIA, DETERMINED BY A COMBINATION OF MASS-SPECTROMETRY AND AUTOMATIC EDMAN DEGRADATION

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 locus Schistocerca gregaria, have been determined. The proteins from the 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.