Characterization of Brucella suis Urease
Author Information
Author(s): Contreras-Rodriguez Araceli, Quiroz-Limon Jose, Martins Ana M, Peralta Humberto, Avila-Calderon Eric, Sriranganathan Nammalwar, Boyle Stephen M, Lopez-Merino Ahide
Primary Institution: Escuela Nacional de Ciencias Biológicas, I.P.N. México
Hypothesis
Only one of the two urease operons in Brucella suis is responsible for encoding an active urease.
Conclusion
The active urease of B. suis is a product of the ure-1 operon, and it has been purified and characterized for the first time.
Supporting Evidence
- The urease was purified 51-fold with a recovery of 12% of the enzyme activity.
- The enzyme showed optimal activity at pH 7.0 and temperatures between 28–35°C.
- The purified enzyme exhibited Michaelis-Menten saturation kinetics with a Km of 5.60 ± 0.69 mM.
Takeaway
Scientists studied a special enzyme from a bacteria that causes brucellosis, and they found out how it works and how it can be recognized by the immune system.
Methodology
The urease was purified using ion exchange and hydrophobic interaction chromatographies, and its activity was measured using spectrophotometric assays.
Limitations
The low concentration of some protein bands made it impossible to sequence them.
Participant Demographics
Sera from 9 patients with brucellosis at different stages of the disease were used.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website