TY - JOUR
T1 - Human sulfatase transiently and functionally active expressed in E. coli K12
AU - Poutou-Piñales, Raúl A.
AU - Vanegas Niño, Adriana
AU - Landázuri, Patricia
AU - Sáenz, Homero
AU - Lareo, Leonardo
AU - Echeverri Peña, Olga Yaneth
AU - Barrera Avellaneda, Luis A.
PY - 2010
Y1 - 2010
N2 - 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.
AB - 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.
KW - E. coli
KW - Glycation
KW - Human sulfatase
KW - Transient expression
UR - http://www.scopus.com/inward/record.url?scp=77954063484&partnerID=8YFLogxK
U2 - 10.2225/vol13-issue3-fulltext-8
DO - 10.2225/vol13-issue3-fulltext-8
M3 - Article
AN - SCOPUS:77954063484
SN - 0717-3458
VL - 13
SP - 1
EP - 10
JO - Electronic Journal of Biotechnology
JF - Electronic Journal of Biotechnology
IS - 3
ER -