Primary structure of apolipophorin-III from the greater wax moth,Galleria mellonella |
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Authors: | Christoph Weise Peter Franke Petr Kopáek and Andreas Wiesner |
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Institution: | (1) Institute of Biochemistry, Free University Berlin, D-14195 Berlin, Germany;(2) Institute of Parasitology, Czech Academy of Sciences, CS-37005 Ceské Budejovice, Czech Republic;(3) Institute of Zoology, Free University Berlin, D-14195 Berlin, Germany |
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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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Keywords: | Galleria mellonella apolipophorin-III Edman sequencing induction of immunity insect immunity |
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