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Isolation, characterization, and N-terminal sequence studies of cuticular proteins from the migratory locust, Locusta migratoria
Article first published online: 3 MAR 2005
DOI: 10.1111/j.1432-1033.1986.tb09371.x
1742-4658/asset/cover.gif?v=1&s=fc98a9fc84ccc5e1b83463cabb40f397544364eb "European Journal of Biochemistry")
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How to Cite
HØJRUP, P., ANDERSEN, S. O. and ROEPSTORFF, P. (1986), Isolation, characterization, and N-terminal sequence studies of cuticular proteins from the migratory locust, Locusta migratoria. European Journal of Biochemistry, 154: 153–159. doi: 10.1111/j.1432-1033.1986.tb09371.x
Publication History
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received July 26/October 17, 1985) – EJB 850830
- Abstract
- Article
- References
- Cited By
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.