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Revista Latinoamericana de Microbiología

2001, Número 2

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Microbiología 2001; 43 (2)


Purificación y caracterización de la Β-lactamasa de Neisseria gonorrhoeae proveniente de muestras clínicas

Castillo MC, Islas MI, Nader OM, Ruiz-Holgado AP

Idioma: Ingles.
Referencias bibliográficas: 33
Paginas: 70-75
Archivo PDF: 135.43 Kb.


RESUMEN

Una Β-lactamasa fue obtenida de Neisseria gonorrhoeae, aislada de pacientes masculinos cun uretritis gonocócica. Las propiedades bioquímicas de la enzima fueron estudiadas. La enzima fue purificada 38 veces usando precipitación con sulfato de amonio, y columnas de Sephadex G-75 y DEAE-celulosa. El extracto purificado exhibió una sola banda por electroforesis en gel de poliacrilamida. La máxima actividad enzimática fue obtenida a 37°C y pH 7.0-7.2 en regulador de fosfatos 50 mM. La adición de Ni2+, Fe2+, Fe3+, Mn2+ and p-chloromercurybenzoate al regulador de la reacción inhibió parcialmente la actividad Β-lactamasa, mientras que el Hg2+ y el EDTA produjeron una inhibición completa. El peso molecular de la enzima se estimó en 35,000 Da y el pI fue de 5.4.


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