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

doi:10.2225/vol13-issue3-fulltext-8

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

Pontificia Universidad Javeriana
Universidad del Quindío
Universidad Centrocidental Lisandro Alvarado

Producción: Contribución a una revista › Artículo › revisión exhaustiva

17 Citas (Scopus)

Resumen

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.

Idioma original	Inglés
Páginas (desde-hasta)	1-10
Número de páginas	10
Publicación	Electronic Journal of Biotechnology
Volumen	13
N.º	3
DOI	https://doi.org/10.2225/vol13-issue3-fulltext-8
Estado	Publicada - 2010

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title = "Human sulfatase transiently and functionally active expressed in E. coli K12",

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.",

keywords = "E. coli, Glycation, Human sulfatase, Transient expression",

author = "Poutou-Pi{\~n}ales, \{Ra{\'u}l A.\} and \{Vanegas Ni{\~n}o\}, Adriana and Patricia Land{\'a}zuri and Homero S{\'a}enz and Leonardo Lareo and \{Echeverri Pe{\~n}a\}, \{Olga Yaneth\} and \{Barrera Avellaneda\}, \{Luis A.\}",

year = "2010",

doi = "10.2225/vol13-issue3-fulltext-8",

language = "English",

volume = "13",

pages = "1--10",

journal = "Electronic Journal of Biotechnology",

issn = "0717-3458",

publisher = "Pontificia Universidad Catolica de Valparaiso",

number = "3",

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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 - https://www.scopus.com/pages/publications/77954063484

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 -

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

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