
doi: 10.1007/bf02780964
pmid: 9853677
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.
Molecular Sequence Data, Mass Spectrometry, Lepidoptera, Molecular Weight, Apolipoproteins, Hemolymph, Manduca, Animals, Amino Acid Sequence, Carrier Proteins, Sequence Alignment, Chromatography, High Pressure Liquid
Molecular Sequence Data, Mass Spectrometry, Lepidoptera, Molecular Weight, Apolipoproteins, Hemolymph, Manduca, Animals, Amino Acid Sequence, Carrier Proteins, Sequence Alignment, Chromatography, High Pressure Liquid
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