Asian Science Citation Index is committed to provide an authoritative, trusted and significant information by the coverage of the most important and influential journals to meet the needs of the global scientific community.  
ASCI Database
308-Lasani Town,
Sargodha Road,
Faisalabad, Pakistan
Fax: +92-41-8815544
Contact Via Web
Suggest a Journal
The Journal of Biochemistry
Year: 2009  |  Volume: 146  |  Issue: 6  |  Page No.: 767 - 769

Expression and Functional Analysis of a Predicted AtsG Arylsulphatase Identified from Mycobacterium tuberculosis Genomic Data

Md. M Hossain, Y Kawarabayasi, M Kimura and Y. Kakuta    

Abstract:

Sulphatase family enzymes hydrolyse the sulphate ester, found on the pathogens cell surface and playing an important role for host–pathogen interaction. The AtsG, homologue of arylsulphatase, predicted in the Mycobacterium tuberculosis genomic data, was successfully expressed in Escherichia coli. The recombinant AtsG protein exhibited hydrolysis of para-nitrophenyl sulphate and para-nitrocatechol sulphate, and binding affinity to the heparin–sepharose resin. This is the first report of molecular evidence for an arylsulphatase activity of the AtsG protein. The maximum activity was detected at pH 8.0 and 37°C. As EDTA completely inhibited this activity, a divalent cation was required for the activity.

View Fulltext    |   Related Articles   |   Back
   
 
 
 
  Related Articles

No Article Found
 
 
 
Copyright   |   Desclaimer   |    Privacy Policy   |   Browsers   |   Accessibility