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 language | English |
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Journal | European Journal of Biochemistry |
Volume | 217 |
Issue number | 1 |
Pages (from-to) | 267-73 |
Number of pages | 7 |
ISSN | 0014-2956 |
DOIs | |
Publication status | Published - 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