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
S. Jespersen et al., 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, Comparative biochemistry and physiology. B. Comparative biochemistry, 109(1), 1994, pp. 125-138
The complete primary structures of two variants of a protein, Abd-5, i
solated from the endocuticles of the migratory locust Locusta migrator
ia and the desert locus Schistocerca gregaria, have been determined. T
he proteins from the the two species are N-terminally blocked with pyr
oglutamic acid. Their sequences differed only in two positions. Compar
ison 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 pos
itions appear to be strictly conserved.