Purification and amino acid composition of peptide antibiotic AS-48 produced by Streptococcus (Enterococcus) faecalis subsp. liquefaciens S-48.

@article{Glvez1989PurificationAA,
  title={Purification and amino acid composition of peptide antibiotic AS-48 produced by Streptococcus (Enterococcus) faecalis subsp. liquefaciens S-48.},
  author={Antonio G{\'a}lvez and Guillermo Gim{\'e}nez-Gallego and Mercedes Maqueda and Eva Valdivia},
  journal={Antimicrobial agents and chemotherapy},
  year={1989},
  volume={33 4},
  pages={437-41}
}
Peptide antibiotic AS-48 was purified to homogeneity by ion-exchange chromatography, gel filtration chromatography, and reversed-phase liquid chromatography. The purified fraction was active against gram-positive and gram-negative bacteria. AS-48 is a basic protein with an isoelectric point of ca. 10.5 and a molecular mass of 7.4 kilodaltons. Its inhibitory activity was markedly affected by sodium dodecyl sulfate and cardiolipin but not by neuraminidase, pectinase, beta-glucosidase, or beta… CONTINUE READING

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