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  • Title: Purification and characterization of beta-lactamase from Neisseria gonorrhoeae from clinical samples.
    Author: de Castillo MC, Islas MI, de Nader OM, de Ruiz-Holgado AP.
    Journal: Rev Latinoam Microbiol; 2001; 43(2):70-5. PubMed ID: 17061490.
    Abstract:
    beta-Lactamase was isolated from Neisseria gonorrhoeae, obtained from male patients with gonococcic urethritis. Biochemical properties of the enzyme were studied. The enzyme was purified 38-fold by ammonium sulphate precipitation and using Sephadex G75 and DEAE-cellulose columns. The purified extract exhibited a single band by polyacrylamide gel electrophoresis. Maximum enzyme activity was obtained at 37 degrees C and pH 7.0-7.2 in 50 mM phosphate buffer. Addition of Ni2+, Fe2+, Fe3+, Mn2+ and p-chloromercurybenzoate to the reaction buffer partially inhibited beta-lactamase activity, whereas Hg2+ and EDTA produced complete inhibition. The molecular weight was estimated to be 35,000 Da and the pI of the enzyme was 5.4.
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