Purification and biological characterization of halocin H1 from Haloferax mediterranei M2a

• Gonzalo Platas ^[1] ; Inmaculada Meseguer ^[2] ; Ricardo Amils ^[1]
  1. [1] Centro de Biología Molecular Severo Ochoa

     Centro de Biología Molecular Severo Ochoa

     Madrid, España

     
  2. [2] Universidad Miguel Hernández de Elche

     Universidad Miguel Hernández de Elche

     Elche, España

     
• Localización: International microbiology: official journal of the Spanish Society for Microbiology, ISSN 1139-6709, Vol. 5, Nº. 1, 2002, págs. 15-19
• Idioma: inglés
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• Resumen

  • The production of halocins, bacteriocin-like proteins of ecological significance, is a frequent characteristic of species from the family Halobacteriaceae. Halocin H1, produced by Haloferax mediterranei strain M2a, is a single 31-kDa polypeptide. Its purification was achieved by combining two chromatographic systems: Sepharose 4B linked to bacitracin followed by hydroxylapatite Bio-gel HTP. Halocin H1 required concentrations of NaCl higher than 1.5 M to maintain its activity. Haoarchaeal strains showed a differential degree of sensitivity to the action of this halocin.