Purification of Penicillin‐Binding Protein 3 from Streptococcus pneumoniae

Abstract

Penicillin‐binding protein 3 from wild‐type Streptococcus pneumoniae has been purified to homogeneity by solubilization with Triton X‐100 and successive column chromatography. The penicillin‐binding activity during the fractionation procedure was monitored with a rapid filter binding assay using [3H]propionylampicillin and penicillin‐binding protein 3 identified after fluorography of dodecyl sulfate gels. The purified protein showed penicillin‐sensitive d, d‐carboxypeptidase activity. Copyright © 1982, Wiley Blackwell. All rights reserved