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

The human iduronate 2-sulfate sulfatase-Like was transiently and functionally active expressed in E. coli K12. The crude extract enzyme activity at 100ml and 400ml oscillated between 0.52 and 4.88nmol h-1 mg-1. The wide Western-blot peptide profile suggest that hrIDS-Like is proteolitically processed ¿randomly¿ which agrees with the ultrafiltration assay in which the hrIDS-Like activity was found in different fractions (100kDa). No glycation sites were found by computer analysis of the hIDS sequence as marks for proteolytic processing.