T. A. Henderson

Penicillin-binding proteins and induction of AmpC beta-lactamase.

Sanders, C C, Bradford, P A, Ehrhardt, A F, Bush, K, Young, K D, Henderson, T A, ...

In competition assays for radiolabeled penicillin, penicillin-binding proteins (PBPs) 4, 7a, and 7b showed very high affinities for strong inducers of AmpC beta-lactamase. Loss of PBP 4 resulted in...

Identification and cloning of the gene encoding penicillin-binding protein 7 of Escherichia coli.

Henderson, T A, Templin, M, Young, K D

Penicillin-binding protein (PBP) 7 of Escherichia coli is a poorly characterized member of the family of enzymes that synthesize and modify the bacterial cell wall. The approximate chromosomal...

AmpC and AmpH, proteins related to the class C beta-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli.

Henderson, T A, Young, K D, Denome, S A, Elf, P K

Two proteins that bind penicillin were observed in Escherichia coli infected with lambda phages 141, 142, 650, and 651 from the Kohara genomic library. These phages carry chromosomal DNA fragments...

Artifactual processing of penicillin-binding proteins 7 and 1b by the OmpT protease of Escherichia coli.

Henderson, T A, Dombrosky, P M, Young, K D

Penicillin-binding proteins (PBPs) were visualized in strains of Escherichia coli that carried mutations in one or more of the following protease genes: tsp, degP, ptr, and ompT. In the absence of a...

Separation of Escherichia coli penicillin-binding proteins into different membrane vesicles by agarose electrophoresis and sizing chromatography.

Leidenix, M J, Jacoby, G H, Henderson, T A, Young, K D

Membrane vesicles from the envelope of Escherichia coli were separated by electrophoresis through dilute agarose and by sizing chromatography through Sephacryl S-1000. These techniques revealed that...

Penicillin-binding proteins and induction of AmpC beta-lactamase.

Sanders, C C, Bradford, P A, Ehrhardt, A F, Bush, K, Young, K D, Henderson, T A, ...

In competition assays for radiolabeled penicillin, penicillin-binding proteins (PBPs) 4, 7a, and 7b showed very high affinities for strong inducers of AmpC beta-lactamase. Loss of PBP 4 resulted in...

Identification and cloning of the gene encoding penicillin-binding protein 7 of Escherichia coli.

Henderson, T A, Templin, M, Young, K D

Penicillin-binding protein (PBP) 7 of Escherichia coli is a poorly characterized member of the family of enzymes that synthesize and modify the bacterial cell wall. The approximate chromosomal...

AmpC and AmpH, proteins related to the class C beta-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli.

Henderson, T A, Young, K D, Denome, S A, Elf, P K

Two proteins that bind penicillin were observed in Escherichia coli infected with lambda phages 141, 142, 650, and 651 from the Kohara genomic library. These phages carry chromosomal DNA fragments...

Artifactual processing of penicillin-binding proteins 7 and 1b by the OmpT protease of Escherichia coli.

Henderson, T A, Dombrosky, P M, Young, K D

Penicillin-binding proteins (PBPs) were visualized in strains of Escherichia coli that carried mutations in one or more of the following protease genes: tsp, degP, ptr, and ompT. In the absence of a...

Separation of Escherichia coli penicillin-binding proteins into different membrane vesicles by agarose electrophoresis and sizing chromatography.

Leidenix, M J, Jacoby, G H, Henderson, T A, Young, K D

Membrane vesicles from the envelope of Escherichia coli were separated by electrophoresis through dilute agarose and by sizing chromatography through Sephacryl S-1000. These techniques revealed that...