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Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella

Authors :
Petr Kopáček
Christoph Weise
Peter Franke
Andreas Wiesner
Source :
Journal of protein chemistry. 17(7)
Publication Year :
1998

Abstract

The complete amino acid sequence of apolipophorin-III (apoLp-III), a lipid-binding hemolymph protein from the greater wax moth, Galleria mellonella, was determined by protein sequencing. The mature protein consists of 163 amino acid residues forming a protein of 18,075.5 Da. Its sequence is similar to apoLp-III from other Lepidopteran species, but remarkably different from the apoLp-IIIs of insects from other orders. As shown by mass spectrometric analysis, the protein carries no modifications. Thus, all of its known physiological functions, including its recently discovered immune response-stimulating activity, must reside in the protein itself.

Details

ISSN :
02778033
Volume :
17
Issue :
7
Database :
OpenAIRE
Journal :
Journal of protein chemistry
Accession number :
edsair.doi.dedup.....c0cc8b702e77be0023e9b04fbabec873