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- W4249286504 abstract "The penicillin binding proteins (PBPs) of 4 representative isolates of Haemophilus influenzae were studied using crude membrane preparations and whole cells grown to the logarithmic and stationary phases of growth. Relative binding, % of total bound, and binding affinities were compared. The PBP patterns were similar for crude membranes and whole cells for all 4 strains tested at each phase of growth. However, PBP 2 was slightly reduced and PBP 4 was markedly reduced with whole-cell labelling in comparison to crude membranes. 8 PBPs were detected in cells labelled during the logarithmic phase of growth, while 6 were detected in stationary phase cells. The pBPs ‘lost’ in stationary phase (PBPs 4 and 6) with apparent Mr of 62 000 and 45 000, respectively, have a high affinity for ampicillin (I50 ≃ 0.04 μg/ml). This suggests that these proteins may have an important role in cell growth, and are targets for β-lactam substrates." @default.
- W4249286504 created "2022-05-12" @default.
- W4249286504 date "2011-05-01" @default.
- W4249286504 modified "2023-09-25" @default.
- W4249286504 title "BP focuses its cellulosic activities on energy grass feedstocks" @default.
- W4249286504 doi "https://doi.org/10.1016/s1351-4180(11)70157-x" @default.
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