Purification of penicillin-binding protein 2 of Escherichia coli.

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Curtis SJ,Strominger JL

doi

10.1128/JB.145.1.398-403.1981

subject

Has Abstract

pub_date

1981-01-01 00:00:00

pages

398-403

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

145

pub_type

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