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In vitro activity of Bay v 3522, a new cephalosporin, compared with activities of other agents
Author(s) -
R. Wise,
J. M. Andrews,
J. P. Ashby,
D. Thornber
Publication year - 1990
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.34.5.813
Subject(s) - bay , microbiology and biotechnology , cefaclor , cephalosporin , penicillin , antibiotics , chemistry , staphylococcus aureus , hydrolysis , haemophilus influenzae , enzyme , bacteria , biology , biochemistry , civil engineering , genetics , engineering
The in vitro activity of Bay v 3522, a new aminobenzothiazol cephem, was compared with those of other oral beta-lactams. Bay v 3522 displayed high activity against Staphylococcus spp. (MICs for 90% of strains tested [MIC90S], 0.5 micrograms/ml), Streptococcus pneumoniae (MIC90, 0.06 micrograms/ml), and Haemophilus influenzae and Branhamella catarrhalis (MIC90S, 2 micrograms/ml). There was limited activity against members of the family Enterobacteriaceae, with the MIC90S being between 4 and greater than 128 micrograms/ml. The stability of Bay v 3522 to hydrolysis by the SHV-1 and TEM-1 enzymes was intermediate to those of cephalexin (least hydrolyzed) and cefaclor, but it was markedly more stable than amoxicillin. There was high affinity to the chromosomally mediated P99 enzyme. The protein binding of Bay v 3522 was 45%. The primary target of Bay v 3522 was penicillin-binding protein 3.

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