Primary structure of apolipophorin-III from the greater wax moth,Galleria mellonella

被引:0
作者
Christoph Weise
Peter Franke
Petr Kopáček
Andreas Wiesner
机构
[1] Free University Berlin,Institute of Biochemistry
[2] Czech Academy of Sciences,Institute of Parasitology
[3] Free University Berlin,Institute of Zoology
来源
Journal of Protein Chemistry | 1998年 / 17卷
关键词
apolipophorin-III; Edman sequencing; induction of immunity; insect immunity;
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摘要
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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页码:633 / 641
页数:8
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