The primary structure of an endocuticular protein from two locust species, Locusta migratoria and Schistocerca gregaria, determined by a combination of mass spectrometry and automatic Edman degradation

Sonja Jespersen, Peter Højrup, Svend Olav Andersen, Peter Roepstorff*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The complete primary structures of two variants of a protein, Abd-5, isolated from the endocuticles of the migratory locust Locusta migratoria and the desert locust Schistocerca gregaria, have been determined. The proteins from the two species are N-terminally blocked with pyroglutamic acid. Their sequences differed only in two positions. Comparison 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 positions appear to be strictly conserved.

Original languageEnglish
JournalComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
Volume109
Issue number1
Pages (from-to)125-138
ISSN1096-4959
DOIs
Publication statusPublished - 1. Jan 1994

Keywords

  • Endocuticular protein
  • Locusta migratoria
  • Schistocerca gregaria

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