Amino acid sequence studies on endocuticular proteins from the desert locust, Schistocerca gregaria.

Seven proteins from the abdominal cuticle of sexually mature locusts, Schistocerca gregaria, have been extracted, purified and sequenced. None of the proteins have been obtained from the pharate adult cuticle of the same species, and they probably represent post-ecdysially deposited endocuticular proteins. All the proteins contain the Rebers-Riddiford consensus sequence commonly found in cuticular proteins. The proteins are all N-terminally blocked by a pyroglutamine residue, and most of them contain one or more N-acetylhexosamine residues, presumably N-acetylgalactosamine (GalNAc), O-linked to either threonine or serine residues. One of the proteins is C-terminally blocked by an amide group. The unglycosylated forms of the proteins have molecular masses in the range from 9 to 20 kDa. The structures of the endocuticular proteins are discussed in relation to the special mechanical properties of locust abdominal cuticle.