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Purification of Penicillin‐Binding Protein 3 from Streptococcus pneumoniae
Author(s) -
HAKENBECK Regine,
KOHIYAMA Masamichi
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb06860.x
Subject(s) - streptococcus pneumoniae , microbiology and biotechnology , penicillin , penicillin binding proteins , antibiotics , chemistry , medicine , biology
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 [ 3 H]propionylampicillin and penicillin‐binding protein 3 identified after fluorography of dodecyl sulfate gels. The purified protein showed penicillin‐sensitive d , d ‐carboxypeptidase activity.

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