Open AccessBiochemical properties and purification of metallo-beta-lactamase from Bacteroides fragilis
Author(s) -
Kaori Bandoh,
Yoshinori Muto,
Kunitomo Watanabe,
Naoki Katoh,
Kazue Ueno
Publication year - 1991
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.35.2.371
Subject(s) - bacteroides fragilis , imipenem , enzyme , bacteroidaceae , bacteroides , microbiology and biotechnology , chemistry , beta lactamase , zinc , biochemistry , molecular mass , antibiotics , biology , bacteria , escherichia coli , organic chemistry , antibiotic resistance , gene , genetics
The beta-lactamase from Bacteroides fragilis GAI-30144 hydrolyzed imipenem, oxyiminocephalosporins, cephamycins, and penicillins. Enzyme activity was inhibited by EDTA. Zinc completely reversed inactivation of the enzyme by EDTA. The molecular mass of purified enzyme was estimated to be 33,000 daltons.