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Resistant penicillin-binding proteins
Cellular and Molecular Life Sciences CMLS, 1998Low-affinity penicillin-binding proteins (PBPs), which participate in the beta-lactam resistance of several pathogenic bacteria, have different origins. Natural transformation and recombination events with DNA acquired from neighbouring intrinsically resistant organisms are responsible for the appearance of mosaic genes encoding two or three low ...
R, Hakenbeck, J, Coyette
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Ion binding of penicillins to proteins
Biochimica et Biophysica Acta (BBA) - General Subjects, 1970Abstract 1. 1. A new method is described, utilising the reactions of hydrated electrons ( e aq − ), to demonstrate that reversible ion binding occurs between a series of penicillins and the proteins, bovine serum albumin and lysozyme. 2. 2.
G O, Phillips +3 more
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Penicillin binding proteins of Vibriocholerae
Biochemical and Biophysical Research Communications, 1990Eleven penicillin binding proteins (PBPs) of Vibrio cholerae have been identified using [125I] labelled p-hydroxybenzyl penicillin (PenX). These proteins are localised in the inner membrane and have molecular weights ranging from 97,000 to 22,000.
T K, Sengupta, A N, Chatterjee, J, Das
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Penicillin-Binding Proteins of Bacteria
1977The penicillin-binding components of bacteria are presumably enzymes of cell wall peptidoglycan synthesis, and one or more of these is a presumed killing site for penicillins. All organisms which have so far been examined contain multiple penicillin-binding components, e.g., there are five in Bacillus subtilis, six in Escherichia coli, and four in ...
J W, Kozarich +4 more
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Penicillin-Binding Proteins in Bacteria
Annals of Internal Medicine, 1982The last 5 to 6 years have witnessed an outburst of renewed interest in the beta-lactam antibiotics. One of the main factors contributing to this was the introduction of the simple and powerful technique of sodium dodecyl sulphate electrophoresis for the identification of bacterial membrane components--penicillin binding proteins--that bind radioactive
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Penicillin‐binding proteins in Listeria monocytogenes
APMIS, 1989The 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 +2 more
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A Method to Assay Penicillin-Binding Proteins
2008Key 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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Affinity of Carumonam for Penicillin-Binding Proteins
Chemotherapy, 1985Direct 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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Synthesis of a 125I-radiolabeled penicillin for penicillin-binding proteins studies
Analytical Biochemistry, 1983Radioiodination 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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