Purification of penicillin-binding protein 3 from Streptococcus pneumoniae.
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.
D001426:Bacterial Proteins / Q000302:isolation & purification*; D002352:Carrier Proteins / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002621:Chemistry; D002845:Chromatography / Q000379:methods; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D013296:Streptococcus pneumoniae / Q000378:metabolism*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase