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. 1994 Mar;176(5):1539–1541. doi: 10.1128/jb.176.5.1539-1541.1994

Construction of a modified penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus and purification by immobilized metal affinity chromatography.

C Y Wu 1, L C Blaszczak 1, M C Smith 1, P L Skatrud 1
PMCID: PMC205227  PMID: 8113200

Abstract

The mecA-27r gene, which encodes PBP2a-27r, was modified by site-specific mutagenesis, resulting in replacement of the N-terminal membrane anchor with a short chelating peptide (CP-PBP2a-27r). CP-PBP2a-27r retained the same binding affinity for beta-lactam antibiotics as the wild-type enzyme. Approximately 95% pure CP-PBP2a-27r was recovered in a single step by use of chelating-peptide-immobilized metal ion affinity chromatography.

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Selected References

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