In vitro investigation of BK-218, a new oral and parenteral cephalosporin.
The antibacterial activity of BK-218 was similar to that of cefamandole when it was tested against several laboratory strains. The inhibiting effect of BK-218 was greater than that of cephalexin and cefoxitin on penicillin-binding proteins of Escherichia coli HB101. This result was in close correlation with the relative inhibition of radiolabeled glucosamine incorporation (greatest with BK-218) and with the lytic effect (most intensive with BK-218). BK-218 proved to be a good inhibitor for all five of the beta-lactamases that were investigated, although two enzymes (Enterobacter cloacae P99 and Pseudomonas aeruginosa Cilote) hydrolyzed it to some extent.
Szabó
I
I
Institute of Biology, University Medical School, Debrecen, Hungary.
Barabás
J
J
Tar
A
A
Kiss
L
L
Filep
M
M
Schmidt
T
T
Marossy
K
K
Tóth-Martinez
B
B
Barabás
G
G
Hernádi
F
F
D001419:Bacteria / Q000187:drug effects* / Q000378:metabolism; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D002511:Cephalosporins / Q000378:metabolism / Q000493:pharmacokinetics / Q000494:pharmacology*; D003593:Cytoplasm / Q000378:metabolism; D013293:Enterococcus faecalis / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D005944:Glucosamine / Q000378:metabolism; D006602:Hexosyltransferases; D008826:Microbial Sensitivity Tests; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D001618:beta-Lactamases / Q000378:metabolism
D001426:Bacterial Proteins; D002352:Carrier Proteins; D002511:Cephalosporins; D046915:Penicillin-Binding Proteins; C063639:BK 218; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D001618:beta-Lactamases; D005944:Glucosamine