Results 261 to 270 of about 635,610 (300)

Penicillin‐binding proteins in Listeria monocytogenes

APMIS, 1989
The Penicillin‐Binding Proteins (PBP) of Listeria monocytogenes 29‐CCM‐A: 454 (ATCC 15313) are described by the use of 125I‐Penicillin X as radiotracer. The membranes of this tolerant bacilli contained at least five proteins with different affinities for the radiotracer or Dicloxacillin. The molecular weights of these proteins were estimated as 76, 74,
G O, Gutkind, M E, Mollerach, R A, De Torres   +2 more
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Affinity of Carumonam for Penicillin-Binding Proteins

Chemotherapy, 1985
Direct labeling experiments with [14C]-carumonam as well as competition binding assays with [14C]-benzylpenicillin and [14C]-ceftriaxone have demonstrated that penicillin-binding protein (PBP) 3 of Escherichia coli, Enterobacter cloacae and Pseudomonas aeruginosa has the highest affinity for carumonam (Ro 17-2301, AMA-1080). PBP 1a is inhibited only at
R L, Then, I, Kohl
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A Method to Assay Penicillin-Binding Proteins

2008
Key enzymes that assemble the bacterial cell wall are also the target of the Beta-lactam class of antibiotics. The covalent binding of labeled penicillin to these proteins has been used in numerous studies in drug discovery, antibiotic mechanisms of action and resistance, and cell wall physiology.
Michael J, Pucci, Thomas J, Dougherty
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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, H.M. Wexler, D. Reeves, S.M. Finegold   +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, Ingrid Van der Westhuyzen   +1 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, Y. R. Cheng, E. Tonin, P. Jacques, FONTANA, Roberta   +4 more
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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, H, Adachi, F, Ishino, M, Matsuhashi, T, Ohta, H, Matsuzawa   +5 more
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Penicillin-Binding Proteins of Gram-Negative Bacteria

Clinical Infectious Diseases, 1988
beta-Lactam antibiotics exert their antibacterial effects by inactivating the high-molecular-weight penicillin-binding proteins (PBPs) that are responsible for the final stages of peptidoglycan biosynthesis. The availability of the amino acid sequences of several low-molecular-weight PBPs, high-molecular-weight PBPs, and active-site serine beta ...
B G, Spratt, K D, Cromie
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Penicillin-binding proteins of Streptococcus pneumoniae

Journal of Antimicrobial Chemotherapy, 1988
Penicillin-binding protein (PBP) patterns of penicillin-resistant laboratory-constructed transformants were compared with the PBP profiles of 26 clinical isolates of Streptococcus pneumoniae. For transformation studies DNA from a penicillin-resistant clinical isolate was used to transform a susceptible laboratory strain.
L J, Chalkley, H J, Koornhof
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Penicillin-binding proteins: evergreen drug targets

Current Opinion in Pharmacology, 2014
The penicillin-binding proteins (PBPs) are well known targets for the β-lactam antibiotics. They continue to be a focus of interest for pharmaceutical design, as exemplified by the number of new agents under clinical investigation as well as novel experimental molecules.
Frère, Jean-Marie, Page, Malcolm G. P.
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