title: Primary structure of a 14 kDa basic structural protein (Lm-76) from the cuticle of the migratory locust, Locusta migratoria.
abstract: The complete amino acid sequence of a 14 kDa structural protein (LM-76) isolated from pharate cuticle of the locust, Locusta migratoria, was determined by Edman degradation of the intact protein and enzymatically derived peptides. Plasma desorption and electrospray mass spectrometry was used as an integrated part of the structure determination. Protein Lm-76 has characteristics similar to proteins previously isolated from the pharate locust. The amino acid composition shows a high content of alanine (32%) and absence of the amino acids Glu, Cys, Met, Phe and Trp. The sequence has a central hydrophilic region surrounded by two hydrophobic regions with 7 repeats of a (Tyr)-Ala-Ala-Pro-Ala/Val motif. The conservation around the prolyl residues within this sequence motif is demonstrated for the hitherto sequenced presumptive exocuticle proteins from L. migratoria. The N-terminal region of protein Lm-76 is enriched in the amino acids Gly, Leu and Tyr located in the conserved sequence NH2-Gly-Tyr-Leu-Gly-Gly-(Tyr)-.
authors: Department of Molecular Biology, Odense University, Denmark.
authors: J S
authors: JS
authors: Andersen
authors: S O
authors: SO
authors: Andersen
authors: P
authors: P
authors: Højrup
authors: P
authors: P
authors: Roepstorff
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002918:Chymotrypsin; D017124:Conserved Sequence; D006110:Grasshoppers / Q000235:genetics*; D019476:Insect Proteins; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D011506:Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D014357:Trypsin
chemical_list: D000596:Amino Acids; D019476:Insect Proteins; D010446:Peptide Fragments; D011506:Proteins; C047663:cuticle proteins, insects; D002918:Chymotrypsin; D014357:Trypsin