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. 1989 Apr;33(4):437-41.
doi: 10.1128/AAC.33.4.437.

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

A Gálvez  1 , G Giménez-Gallego, M Maqueda, E Valdivia
Affiliations

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

A Gálvez et al. Antimicrob Agents Chemother. 1989 Apr.

Abstract

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-glucuronidase. Differential scanning calorimetry data suggested that AS-48 molecules lack a compact structure.

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