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

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 proteoli...

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Autores principales:	Poutou-Piñales,Raúl A, Vanegas Niño,Adriana, Landázuri,Patricia, Sáenz,Homero, Lareo,Leonardo, Echeverri Peña,Olga Yaneth, Barrera Avellaneda,Luis A
Lenguaje:	English
Publicado:	Pontificia Universidad Católica de Valparaíso 2010
Materias:	E. coli glycation human sulfatase transient expression
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000300005
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spelling	oai:scielo:S0717-345820100003000052010-06-08Human sulfatase transiently and functionally active expressed in E. coli K12Poutou-Piñales,Raúl AVanegas Niño,AdrianaLandázuri,PatriciaSáenz,HomeroLareo,LeonardoEcheverri Peña,Olga YanethBarrera Avellaneda,Luis A E. coli glycation human sulfatase transient expression 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.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.13 n.3 20102010-05-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000300005en
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	E. coli glycation human sulfatase transient expression
spellingShingle	E. coli glycation human sulfatase transient expression Poutou-Piñales,Raúl A Vanegas Niño,Adriana Landázuri,Patricia Sáenz,Homero Lareo,Leonardo Echeverri Peña,Olga Yaneth Barrera Avellaneda,Luis A Human sulfatase transiently and functionally active expressed in E. coli K12
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.
author	Poutou-Piñales,Raúl A Vanegas Niño,Adriana Landázuri,Patricia Sáenz,Homero Lareo,Leonardo Echeverri Peña,Olga Yaneth Barrera Avellaneda,Luis A
author_facet	Poutou-Piñales,Raúl A Vanegas Niño,Adriana Landázuri,Patricia Sáenz,Homero Lareo,Leonardo Echeverri Peña,Olga Yaneth Barrera Avellaneda,Luis A
author_sort	Poutou-Piñales,Raúl A
title	Human sulfatase transiently and functionally active expressed in E. coli K12
title_short	Human sulfatase transiently and functionally active expressed in E. coli K12
title_full	Human sulfatase transiently and functionally active expressed in E. coli K12
title_fullStr	Human sulfatase transiently and functionally active expressed in E. coli K12
title_full_unstemmed	Human sulfatase transiently and functionally active expressed in E. coli K12
title_sort	human sulfatase transiently and functionally active expressed in e. coli k12
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2010
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000300005
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Human sulfatase transiently and functionally active expressed in E. coli K12

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