Combined plasma-desorption mass spectrometry and Edman degradation applied to simultaneous sequence determination of isoforms of structural proteins from the cuticle of Locusta migratoria

L Andreasen, P Højrup, S O Andersen, P Roepstorff

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The primary structures of two basic low-molecular-mass proteins, Lm-67 and Lm-70 from the pharate cuticle of the migratory locust, Locusta migratoria, were determined. The sequencing strategy was based on combined use of plasma--desorption mass spectrometry (PDMS) and automatic Edman degradation of the proteins and their enzymically derived peptides. The mass-spectral data showed the presence of two proteins in each preparation. For protein preparation Lm-67, this was indicated by the mass spectrum of the intact protein. For protein preparation Lm-70, the presence of two variants only became evident by mass-spectrometric analysis of the enzymically derived peptides. Both proteins show strong similarity to other exocuticular proteins from L. migratoria.

Original languageEnglish
JournalEuropean Journal of Biochemistry
Volume217
Issue number1
Pages (from-to)267-73
Number of pages7
ISSN0014-2956
DOIs
Publication statusPublished - 1. Oct 1993

Keywords

  • Amino Acid Sequence
  • Animals
  • Chromatography, High Pressure Liquid
  • Chymotrypsin/metabolism
  • Grasshoppers/chemistry
  • Insect Hormones/chemistry
  • Insect Proteins
  • Mass Spectrometry
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments/chemistry
  • Sequence Analysis/methods
  • Trypsin/metabolism

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