Phenoloxidase in the hemolymph of Sarcophaga bullata larvae is present as an inactive proenzyme form. Localization studies indicate that the majority of the prophenoloxidase is present in the plasma fraction whereas only a minor fraction (about 4%) is present in the cellular compartments (hemocytes)
Mapping the peptide and protein immune response in the larvae of the fleshfly Sarcophaga bullata
✍ Scribed by Alice Ciencialová; Tereza Neubauerová; Miloslav Šanda; Radek Šindelka; Josef Cvačka; Zdeněk Voburka; Miloš Buděšínský; Václav Kašička; Petra Sázelová; Veronika Šolínová; Martina Macková; Bohumír Koutek; Jiří Jiráček
- Publisher
- John Wiley and Sons
- Year
- 2008
- Tongue
- English
- Weight
- 401 KB
- Volume
- 14
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.967
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✦ Synopsis
Abstract
We chose the larvae of fleshfly Sarcophaga bullata to map the peptide and protein immune response. The hemolymph of the third‐instar larvae of S. bullata was used for isolation. The larvae were injected with bacterial suspension to induce an antimicrobial response. The hemolymph was separated into crude fractions, which were subdivided by RP‐HPLC, gel electrophoresis, and free‐flow electrophoresis. In several fractions, we determined significant antimicrobial activities against the pathogenic bacteria Escherichia coli, Staphylococcus aureus, or Pseudomonas aeruginosa. Among antimicrobially active compounds we identified dipeptide β‐alanyl‐ L‐tyrosine, protein transferrin, and two variants of peptide sapecin. We also partially characterized two novel antimicrobially active polypeptides; odorant‐binding protein 99b, and a peptide which remains unidentified. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.
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