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

Raúl A. Poutou-Piñales, Adriana Vanegas Niño, Patricia Landázuri, Homero Sáenz, Leonardo Lareo, Olga Yaneth Echeverri Peña, Luis A. Barrera Avellaneda

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)1-10
Number of pages10
JournalElectronic Journal of Biotechnology
Volume13
Issue number3
DOIs
StatePublished - 2010

Keywords

  • E. coli
  • Glycation
  • Human sulfatase
  • Transient expression

Fingerprint

Dive into the research topics of 'Human sulfatase transiently and functionally active expressed in E. coli K12'. Together they form a unique fingerprint.

Cite this