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

被引:32
作者
Weise, C
Franke, P
Kopacek, P
Wiesner, A [1 ]
机构
[1] Free Univ Berlin, Inst Zool, D-14195 Berlin, Germany
[2] Free Univ Berlin, Inst Biochem, D-14195 Berlin, Germany
[3] Acad Sci Czech Republ, Inst Parasitol, CS-37005 Ceske Budejovice, Czech Republic
来源
JOURNAL OF PROTEIN CHEMISTRY | 1998年 / 17卷 / 07期
关键词
Galleria mellonella; apolipophorin-III; Edman sequencing; induction of immunity; insect immunity;
D O I
10.1007/BF02780964
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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. fts 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.
引用
收藏
页码:633 / 641
页数:9
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