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

      Journal of protein chemistry
      Amino Acid Sequence, Animals, Apolipoproteins, chemistry, isolation & purification, Carrier Proteins, Chromatography, High Pressure Liquid, Hemolymph, Lepidoptera, Manduca, Mass Spectrometry, Molecular Sequence Data, Molecular Weight, Sequence Alignment

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          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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