| Literature DB >> 9853677 |
C Weise1, P Franke, P Kopácek, A Wiesner.
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.Entities:
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Year: 1998 PMID: 9853677 DOI: 10.1007/bf02780964
Source DB: PubMed Journal: J Protein Chem ISSN: 0277-8033