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. 1981 Jan;145(1):398–403. doi: 10.1128/jb.145.1.398-403.1981

Purification of penicillin-binding protein 2 of Escherichia coli.

S J Curtis, J L Strominger
PMCID: PMC217285  PMID: 7007320

Abstract

Penicillin-binding protein 2 (PBP-2) of Escherichia coli K-12 was purified by covalent affinity chromatography using 6-aminopenicillanic acid covalently coupled to carboxymethyl-Sepharose (6-APA-CM-Sepharose). Purification of PBP-2 was accomplished by prebinding the methoxy cephalosporin, cefoxitin, to the Triton X-100-solubilized PBPs of E. coli and then incubating the PBPs with 6-APA-CM-Sepharose. Cefoxitin readily binds to all the E. coli PBPs except PBP-2 and, thus, in the presence of cefoxitin, only PBP-2 could bind to the 6-APA-CM-Sepharose. The purification of a mixture of all of the PBPs of E. coli by affinity chromatography is also described.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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