Open AccessIsolation, characterization, and N‐terminal sequence studies of cuticular proteins from the migratory locust, Locusta migratoria
Author(s) -
HØJRUP Peter,
ANDERSEN Svend Olav,
ROEPSTORFF Peter
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb09371.x
Subject(s) - locust , migratory locust , amino acid , biology , biochemistry , peptide sequence , alanine , glycine , cuticle (hair) , tyrosine , leucine , botany , anatomy , gene
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.