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.
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Weise, C., Franke, P., Kopáček, P. et al. Primary structure of apolipophorin-III from the greater wax moth,Galleria mellonella. J Protein Chem 17, 633–641 (1998). https://doi.org/10.1007/BF02780964
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DOI: https://doi.org/10.1007/BF02780964