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of 32
pro vyhledávání: '"Hans Herbert Martin"'
Autor:
Jean-Marie Frère, Moreno Galleni, Jozef Van Beeumen, Bernard Joris, Essam A. M. Azab, Martina Datz, Hans Herbert Martin
Publikováno v:
European Journal of Biochemistry. 226:149-157
Among the Enterobacteriaceae, Proteus vulgaris is exceptional in the inducible production of a 29-kDa β-lactamase (cefuroximase) with an unusually high activity towards the β-lactamase-stable oximino-cephalosporins (e.g. cefuroxime and cefotaxime).
Publikováno v:
Journal of Antimicrobial Chemotherapy. 41:189-195
Using clinical strains of Serratia marcescens with low and high resistance to extended-spectrum beta-lactam antibiotics, the relative contribution of chromosomal beta-lactamase and defective outer membrane porins to resistance was determined. Low-lev
Autor:
Herbert Schmidt, Staffan Normark, Susanne Lindquist, Kathleen Weston-Hafer, Hans Herbert Martin, Christian Pul, Gisela Korfmann, Christine C. Sanders, Jay Erickson
Publikováno v:
Molecular Microbiology. 9:703-715
The chromosomal ampC beta-lactamase in Citrobacter freundii and Enterobacter cloacae is inducible by beta-lactam antibiotics. When an inducible ampC gene is introduced on a plasmid into Escherichia coli together with its transcriptional regulator amp
Autor:
Hans Herbert Martin
Publikováno v:
Archives of microbiology. 192(3)
Publikováno v:
Microbiology (Reading, England). 141
SUMMARY Chemical mutagenesis of the AmpC -lactamase-hyperinducible Escherichia coli strain SN0301/pNu305 carrying the cloned ampC and ampR genes from Citrobacter freundii OS60 gave four independent mutants in which -lactamase was no longer inducible,
Publikováno v:
Journal of general microbiology. 139(11)
The mobilizable plasmid pMD101 (ampR, ampC) was constructed by inserting cloned ampC, the structural gene for the chromosomal AmpC beta-lactamase of Citrobacter freundii, and the closely linked ampR encoding the transcriptional regulator essential fo
Autor:
Herbert Schmidt, Hans Herbert Martin
Publikováno v:
Bacterial Growth and Lysis ISBN: 9781475793611
It has been reasoned that bacterial β-lactamases must have a “normal” physiological function, apart from inactivating β-lactam antibiotics, probably connected to the metabolism of cell wall peptidoglycan (Abraham and Chain, 1940; Saz and Lowery
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3d60561a840b3f8c791a4dabaf36154a
https://doi.org/10.1007/978-1-4757-9359-8_40
https://doi.org/10.1007/978-1-4757-9359-8_40
Publikováno v:
Journal of general microbiology. 137(12)
SUMMARY: A serum-resistant strain of Proteus mirabilis was used to determine whether changes in the composition of surface components could be detected following induction of progressive stages of cell form defectiveness by β-lactam antibiotics. The
Publikováno v:
Journal of general microbiology. 137(2)
The quantities of penicillin-binding proteins (PBPs), and sensitivity to extended-spectrum β-lactams, were measured in isogenic strains of Serratia marcescens with high (HR) and low (LR) resistance to extended-spectrum β-lactam antibiotics and with
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 510:87-98
In the presence of MgCl2, amounts of detergents which disrupted phospholipid vesicles caused lipopolysaccharide I from Proteus mirabilis to aggregate and form vesicular, membrane-like structures. Vesicle formation with P. mirabilis lipopolysaccharide