Human sulfatase transiently and functionally active expressed in E. coli K12

• Raúl A Poutou-Piñales ^[1] ; Adriana Vanegas Niño ^[1] ; Patricia Landázuri ^[2] ; Homero Sáenz ^[1] ; Leonardo Lareo ^[1] ; Olga Yaneth Echeverri Peña ^[1] ; Luis A Barrera Avellaneda ^[1]
  1. [1] Pontífica Universidad Javeriana

     Pontífica Universidad Javeriana

     Colombia

     
  2. [2] Universidad del Quindío

     Universidad del Quindío

     Colombia

     
• Localización: Electronic Journal of Biotechnology, ISSN-e 0717-3458, Vol. 13, Nº. 3, 2010, págs. 5-6
• Idioma: inglés
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• Resumen

  • The recombinant human iduronate 2-sulfate sulfatase (hrIDS) was transiently and functionally active expressed in E. coli K12. The enzyme activity (crude extract) at 100 ml and 400 ml oscillated between 0.25 and 10.58 nmol h-1 mg-1. The wide Western-blot peptide profile suggest that hrIDS is proteolitically processed “randomly” which agrees with the ultrafiltration assay in which the hrIDS activity was found in all fractions (<30kDa, 30-100kDa and >100kDa). No glycation sites were found by computer analysis of the hIDS sequence; discarding the possibility of marks for glycation and proteolytic processing.