Results 261 to 270 of about 384,367 (304)

Penicillin binding proteins of Vibriocholerae

Biochemical and Biophysical Research Communications, 1990
Eleven 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 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 Bacteria

1977
The 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, C E, Buchanan, S J, Curtis, S, Hammarström, J L, Strominger   +4 more
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Ion binding of penicillins to proteins

Biochimica et Biophysica Acta (BBA) - General Subjects, 1970
Abstract 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, D M, Power, C, Robinson, J V, Davies   +3 more
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Penicillin-Binding Proteins in Bacteria

Annals of Internal Medicine, 1982
The 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: 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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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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Variability of Penicillin-Binding Proteins from Penicillin-Sensitive Streptococcus pneumoniae

Journal of Infectious Diseases, 1991
Penicillin-binding proteins (PBPs) from penicillin-susceptible strains of Streptococcus pneumoniae are believed to be fairly similar in contrast to PBPs occurring in resistant isolates. The antigenic variation of PBPs 1a and 2b in 65 penicillin-susceptible strains from different geographic areas and a wide variety of isolation sites was analyzed using ...
Hakenbeck R, Briese T, Chalkley L, Ellerbrok H, Kalliokoski R, Latorre C, Leinonen M, Martin C   +7 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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Penicillin-binding proteins ofRhodospirillum rubrum

Current Microbiology, 1988
Four major pencillin-binding proteins (PBPs) were detected in membranes ofRhodospirillum rubrum labeled with radioiodinated penicillin X. These PBPs were localized primarily in the cytoplasmic membrane of aerobic cells, which had a higher content of PBPs relative to protein than did the outer membrane or a hybrid fraction containing both cytoplasmic ...
Charles R. Myers, Mary Lynne Perille Collins   +1 more
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