Isolation, characterization, and N-terminal sequence studies of cuticular proteins from the migratory locust, Locusta migratoria

Abstract

The cuticle of the migratory locust, Locusta migratoria, contains more than a hundred different structural proteins, which can be extracted before but not after the cuticle is sclerotized. Fourteen of the proteins have been purified, covering a pI range of 6.4–10.6 and a molecular mass range of 15.2–36.8 kDa. The amino acid sequence from the N-terminal, ranging in length over 10–59 residues, have been obtained for eight of the proteins. A number of similarities, both in amino acid composition and in sequences, indicate that the proteins belong to a new protein family, characterized by an N-terminal part which is rich either in glycine, tyrosine and leucine or in hydrophilic amino acids, followed by a very alanine-rich portion. Similarities between this family of proteins and other structural proteins from insects are discussed.