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Journal of Protein Chemistry

, Volume 17, Issue 7, pp 633–641 | Cite as

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

  • Christoph Weise
  • Peter Franke
  • Petr Kopáček
  • Andreas Wiesner
Article

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.

Key words

Galleria mellonella apolipophorin-III Edman sequencing induction of immunity insect immunity 

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Copyright information

© Plenum Publishing Corporation 1998

Authors and Affiliations

  • Christoph Weise
    • 1
  • Peter Franke
    • 1
  • Petr Kopáček
    • 2
  • Andreas Wiesner
    • 3
  1. 1.Institute of BiochemistryFree University BerlinBerlinGermany
  2. 2.Institute of ParasitologyCzech Academy of SciencesCeské BudejoviceCzech Republic
  3. 3.Institute of ZoologyFree University BerlinBerlinGermany

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