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. 2001 Apr-Jun;43(2):70-5.

Purification and characterization of beta-lactamase from Neisseria gonorrhoeae from clinical samples

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  • PMID: 17061490

Purification and characterization of beta-lactamase from Neisseria gonorrhoeae from clinical samples

M C de Castillo et al. Rev Latinoam Microbiol. 2001 Apr-Jun.

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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