Affinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K-12 and their antibacterial activity.
AUTOR(ES)
Curtis, N A
RESUMO
The affinities of a range of penicillins and cephalosporins for ther penicillin-binding proteins of Escherichia coli K-12 have been studied, and the results were compared with the antibacterial activity of the compounds against E. coli K-12 and an isogenic permeability mutant. Different penicillins and cephalosporins exhibited different affinities for the "essential" penicillin-binding proteins of E. coli K-12, in a manner which directly correlated with their observed effects upon bacterial morphology. Furthermore, the affinities of the compounds for their "primary" lethal penicillin-binding protein targets showed close agreement with their antibacterial activities against the permeability mutant.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=352901Documentos Relacionados
- Affinity of temocillin for Escherichia coli K-12 penicillin-binding proteins.
- Comparison of cefepime, cefpirome, and cefaclidine binding affinities for penicillin-binding proteins in Escherichia coli K-12 and Pseudomonas aeruginosa SC8329.
- Binding of Thienamycin and Clavulanic Acid to the Penicillin-Binding Proteins of Escherichia coli K-12
- Inhibition of Escherichia coli K-12 by β-Lactam Antibiotics With Poor Antibacterial Activity: Interaction of Permeability And Intrinsic Activity Against Penicillin-Binding Proteins
- Inhibition of Escherichia coli K-12 by β-Lactam Antibiotics With Poor Antibacterial Activity: Interaction of Permeability and Intrinsic Activity Against Penicillin-Binding Proteins