Combined plasma-desorption mass spectrometry and Edman degradation applied to simultaneous sequence determination of isoforms of structural proteins from the cuticle of Locusta migratoria.
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.
Andreasen
L
L
Department of Molecular Biology, Odense University, Denmark.
Højrup
P
P
Andersen
S O
SO
Roepstorff
P
P
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000378:metabolism; D006110:Grasshoppers / Q000737:chemistry*; D007301:Insect Hormones / Q000737:chemistry* / Q000302:isolation & purification; D019476:Insect Proteins; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D017421:Sequence Analysis / Q000379:methods*; D014357:Trypsin / Q000378:metabolism
D007301:Insect Hormones; D019476:Insect Proteins; C083935:Lm-67 protein, Locusta migratoria; C083936:Lm-70 protein, Locusta migratoria; D010446:Peptide Fragments; D002918:Chymotrypsin; D014357:Trypsin