[Physico-chemical and enzymological properties of beta-lactamase from Bacteroides fragilis].
Bacteroides fragilis 55 from clinical specimens was selected at random for beta-lactamase investigation of physico-chemical and enzymological properties. The enzyme was characterized as a cell-associated cephalosporinase with some penicillinase activity, the molecular weight of the enzyme being 43,000 and the pI 4.95. It could be inhibited by cefoxitin, PCMB, carbenicillin, sulbactam, clavulanic acid and cloxacillin. The optimum pH and temperature for enzyme reactions have been found to be 7.2 and 37 degrees C, respectively. The analysis of amino acid composition and parameters of enzyme kinetics has been described.
Chen
J
J
Institute of Epidemiology and Microbiology, Academy of Preventive Medicine, Beijing.
Liu
B
B
Bao
Y
Y
D000596:Amino Acids / Q000032:analysis; D001441:Bacteroides fragilis / Q000201:enzymology*; D007700:Kinetics; D008970:Molecular Weight; D001618:beta-Lactamases / Q000737:chemistry* / Q000302:isolation & purification
D000596:Amino Acids; D001618:beta-Lactamases