Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella.
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.
Weise
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C
Institute of Biochemistry, Free University Berlin, Germany.
Franke
P
P
Kopácek
P
P
Wiesner
A
A
D000595:Amino Acid Sequence; D000818:Animals; D001053:Apolipoproteins / Q000737:chemistry* / Q000302:isolation & purification; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002851:Chromatography, High Pressure Liquid; D006458:Hemolymph / Q000737:chemistry; D007915:Lepidoptera / Q000737:chemistry*; D018402:Manduca; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016415:Sequence Alignment
D001053:Apolipoproteins; D002352:Carrier Proteins; C042470:apolipophorin III