beta-Lactamase activity in human pus.
Pus was obtained from patients with polymicrobial intraabdominal abscesses or polymicrobial empyema. Physical and chemical characteristics of 12 specimens were examined, and bacterial isolates were enumerated. Pus supernatant of six specimens rapidly inactivated penicillin, cephalothin, and cefazolin. Carbenicillin and ticarcillin were similarly degraded by supernatant of certain pus specimens. Cefoxitin, chloramphenicol, and clindamycin were not appreciably inactivated by pus supernatant. Degradation of penicillin and cephalosporin congeners in pus was due to the presence of beta-lactamase, as shown by chemical interaction with nitrocefin, chromatography, and inhibition by the beta-lactamase inhibitor clavulanic acid. Pus supernatant containing beta-lactamase activity reduced the bactericidal activity of carbenicillin against Bacteroides fragilis in whole pus in an abscess model in vitro. Bactericidal activity of clindamycin or cefoxitin was not impaired in pus containing beta-lactamase.
D001441:Bacteroides fragilis; D002437:Cefazolin / Q000494:pharmacology; D002512:Cephalothin / Q000494:pharmacology; D055598:Chemical Phenomena; D002621:Chemistry; D002854:Chromatography, Paper; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008826:Microbial Sensitivity Tests; D009994:Osmolar Concentration; D010400:Penicillin G / Q000494:pharmacology; D013492:Suppuration / Q000201:enzymology* / Q000382:microbiology; D001618:beta-Lactamases / Q000378:metabolism*
D001618:beta-Lactamases; D002437:Cefazolin; D010400:Penicillin G; D002512:Cephalothin