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

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Abstract
Peptide antibiotic AS-48 was purified to homogeneity by ion-exchange chromatograpy, gel filtration chromatography, an 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.-glucuronidiase. Differential scanning calorimetry data suggested that AS-48 molecules lack a compact structure.