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

dc.creator	Poutou-Piñales,Raúl A
dc.creator	Vanegas Niño,Adriana
dc.creator	Landázuri,Patricia
dc.creator	Sáenz,Homero
dc.creator	Lareo,Leonardo
dc.creator	Echeverri Peña,Olga Yaneth
dc.creator	Barrera Avellaneda,Luis A
dc.date	2010-05-01
dc.date.accessioned	2019-05-03T12:44:43Z
dc.date.available	2019-05-03T12:44:43Z
dc.identifier	https://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000300005
dc.identifier.uri	http://revistaschilenas.uchile.cl/handle/2250/85124
dc.description	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.
dc.format	text/html
dc.language	en
dc.publisher	Pontificia Universidad Católica de Valparaíso
dc.rights	info:eu-repo/semantics/openAccess
dc.source	Electronic Journal of Biotechnology v.13 n.3 2010
dc.subject	E. coli
dc.subject	glycation
dc.subject	human sulfatase
dc.subject	transient expression
dc.title	Human sulfatase transiently and functionally active expressed in E. coli K12