PRIMARY STRUCTURE OF APOLIPOPHORIN-III FROM THE GREATER WAX MOTH, GALLERIA-MELLONELLA

The complete amino acid sequence of apolipophorin-III (apoLp-III), a l ipid-binding hemolymph protein from the greater wax moth, Galleria mel lonella, was determined by protein sequencing. The mature protein cons ists of 163 amino acid residues forming a protein of 18,075.5 Da. fts 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 modif ications. Thus, all of its known physiological functions, including it s recently discovered immune response-stimulating activity, must resid e in the protein itself.