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Synthesis of a 125I-radiolabeled penicillin for penicillin-binding proteins studies

Analytical Biochemistry, 1983
Radioiodination of penicillin X (p-hydroxybenzylpenicillin) with 125INa, using the chloramine-T method, is simple and almost quantitative. The product thus obtained can be used without further purification for the penicillin-binding proteins (PBPs) assay.
J M, Masson, R, Labia
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Identification of the Penicillin-Binding Active Site of Penicillin-Binding Protein 2 of Escherichia coli

The Journal of Biochemistry, 1988
We determined the active site of penicillin-binding protein (PBP) 2 of Escherichia coli. A water-soluble form of PBP 2, which was constructed by site-directed mutagenesis, was purified by affinity chromatography, labeled with dansyl-penicillin, and then digested with a combination of proteases.
A, Takasuga   +5 more
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Purification of Streptococcus faecium penicillin binding protein 5, a multifunctional penicillin-binding protein.

Microbiologica, 1986
Penicillin-binding protein 5 of Streptococcus faecium has been solubilized and partially separated from other membrane proteins by covalent affinity chromatography. PBP 5 was successively purified to homogeneity by resolution on SDS-polyacrylamide gel, elution and renaturation of penicillin-binding activity.
A. Grossato   +4 more
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Penicillin-Binding Proteins inFusobacteriumSpecies

Anaerobe, 1996
Abstract PBPs were identified in four species ofFusobacterium. Each species had a distinctive PBP pattern, although some intra-species variation was noted. Most species had five or six PBPs, ranging in molecular weight from ∼100 kDa to ∼40 kDa. The two strains ofF. nucleatumtested had characteristic “wavy” PBP patterns.F. mortiferumwas distinctive in
K. Tunér   +3 more
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Penicillin-binding proteins of clostridia

Current Microbiology, 1993
The penicillin-binding protein (PBP) profiles of 33Clostridium perfringens and sixClostridium species isolated from clinically significant infections were analyzed. Three new PBPs—PBPs 2B, 4B, and 5B (84, 70, and 49 kDa respectively)—and a high-molecular-weight PBP 6 (45 kDa) were demonstrated in theC. perfringens isolates. In addition to PBPs 1 and 2,
Lynda Chalkley   +1 more
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