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Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella
- Source :
- Journal of protein chemistry. 17(7)
- Publication Year :
- 1998
-
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.
- Subjects :
- animal structures
Molecular Sequence Data
Sequence alignment
Biology
Biochemistry
Mass Spectrometry
Protein sequencing
Hemolymph
Manduca
Animals
Amino Acid Sequence
Peptide sequence
Chromatography, High Pressure Liquid
Edman degradation
fungi
Protein primary structure
biology.organism_classification
Galleria mellonella
Lepidoptera
Molecular Weight
Apolipoproteins
Apolipophorin III
Carrier Proteins
Sequence Alignment
Subjects
Details
- ISSN :
- 02778033
- Volume :
- 17
- Issue :
- 7
- Database :
- OpenAIRE
- Journal :
- Journal of protein chemistry
- Accession number :
- edsair.doi.dedup.....c0cc8b702e77be0023e9b04fbabec873