Title: Purification and characterization of a cysteine‐rich 11.5‐kDa antibacterial protein from the granular haemocytes of the shore crab, <i>Carcinus maenas</i>
Abstract: Extracts of the granular haemocytes of Carcinus maenas were subjected to ion‐exchange chromatography and reverse‐phase (RP)‐HPLC to investigate the presence of an antibacterial protein of ≈ 11 kDa. This protein was isolated, characterized and subjected to partial amino acid sequence analysis. It was found by mass spectrometry to have a molecular mass of 11 534 Da, to be cationic and hydrophobic and active only against marine Gram‐positive bacteria. In addition its activity is stable after heating to 100 °C and is retained at concentrations as low as 10 µg·mL −1 . It has an unusual amino acid sequence, unlike any known antibacterial peptide described in the literature but bears a consensus disulphide domain signature, indicating that it might be a member of the four‐disulphide core proteins. Partial cDNA sequence data has been obtained.
Publication Year: 1999
Publication Date: 1999-09-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
Access and Citation
Cited By Count: 240
AI Researcher Chatbot
Get quick answers to your questions about the article from our AI researcher chatbot