Primary structure of apolipophorin-III from the greater wax moth,Galleria mellonella |
| |
Authors: | Christoph Weise Peter Franke Petr Kopáček Andreas Wiesner |
| |
Affiliation: | (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 |
| |
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. |
| |
Keywords: | Galleria mellonella apolipophorin-III Edman sequencing induction of immunity insect immunity |
本文献已被 SpringerLink 等数据库收录! |
|