title: Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella.
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.
authors.affiliation: Institute of Biochemistry, Free University Berlin, Germany.
authors.forename: C
authors.initials: C
authors.lastname: Weise
authors.forename: P
authors.initials: P
authors.lastname: Franke
authors.forename: P
authors.initials: P
authors.lastname: Kopácek
authors.forename: A
authors.initials: A
authors.lastname: Wiesner
mesh_terms: 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
chemical_list: D001053:Apolipoproteins; D002352:Carrier Proteins; C042470:apolipophorin III