Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from α-macroglobulins

Daniel Iván Barrera, Luisa Marina Matheus, Torgny Stigbrand, Luis Fernando Arbeláez

Resultado de la investigación: Contribución a RevistaArtículo

4 Citas (Scopus)

Resumen

A new, easier and efficient purification method, using Sephacryl and DEAE-Sephacel, of the C-terminal fragment of two α-macroglobulins, α2-M and PZP, is presented. Two larger peptides were identified for each protein as the C-terminal fragment, with molecular weights of ∼30 kDa and the N-terminal sequences were determined to be SSTQDTV for α2-M and VALHLS for PZP. The smaller peptides with molecular weights of 18 kDa correspond to a shorter C-terminal sequence of these proteins, and they were determined to be EEFPFA for α2-M and ALKVQTV for PZP, with no interfering sequences detected. The results confirmed the discriminatory capacity of the purification procedure and the purity of the fragments. This new methodology facilitates biological studies of α-macroglobulins, and will enable elucidation of the role the C-terminal region may exert to eliminate α-macroglobulin-proteinases complexes from the circulation by the LRP/receptor. © 2006 Elsevier Inc. All rights reserved.
Idioma originalEnglish (US)
Páginas (desde-hasta)112-118
Número de páginas7
PublicaciónProtein Expression and Purification
DOI
EstadoPublished - may 1 2007

Huella dactilar

Low Density Lipoprotein Receptor-Related Protein-1
alpha-Macroglobulins
Hydrolysis
Molecular Weight
Peptides
Protein C
Peptide Hydrolases
Proteins

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title = "Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from α-macroglobulins",
abstract = "A new, easier and efficient purification method, using Sephacryl and DEAE-Sephacel, of the C-terminal fragment of two α-macroglobulins, α2-M and PZP, is presented. Two larger peptides were identified for each protein as the C-terminal fragment, with molecular weights of ∼30 kDa and the N-terminal sequences were determined to be SSTQDTV for α2-M and VALHLS for PZP. The smaller peptides with molecular weights of 18 kDa correspond to a shorter C-terminal sequence of these proteins, and they were determined to be EEFPFA for α2-M and ALKVQTV for PZP, with no interfering sequences detected. The results confirmed the discriminatory capacity of the purification procedure and the purity of the fragments. This new methodology facilitates biological studies of α-macroglobulins, and will enable elucidation of the role the C-terminal region may exert to eliminate α-macroglobulin-proteinases complexes from the circulation by the LRP/receptor. {\circledC} 2006 Elsevier Inc. All rights reserved.",
author = "Barrera, {Daniel Iv{\'a}n} and Matheus, {Luisa Marina} and Torgny Stigbrand and Arbel{\'a}ez, {Luis Fernando}",
year = "2007",
month = "5",
day = "1",
doi = "10.1016/j.pep.2006.12.008",
language = "English (US)",
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journal = "Protein Expression and Purification",
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Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from α-macroglobulins. / Barrera, Daniel Iván; Matheus, Luisa Marina; Stigbrand, Torgny; Arbeláez, Luis Fernando.

En: Protein Expression and Purification, 01.05.2007, p. 112-118.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from α-macroglobulins

AU - Barrera, Daniel Iván

AU - Matheus, Luisa Marina

AU - Stigbrand, Torgny

AU - Arbeláez, Luis Fernando

PY - 2007/5/1

Y1 - 2007/5/1

N2 - A new, easier and efficient purification method, using Sephacryl and DEAE-Sephacel, of the C-terminal fragment of two α-macroglobulins, α2-M and PZP, is presented. Two larger peptides were identified for each protein as the C-terminal fragment, with molecular weights of ∼30 kDa and the N-terminal sequences were determined to be SSTQDTV for α2-M and VALHLS for PZP. The smaller peptides with molecular weights of 18 kDa correspond to a shorter C-terminal sequence of these proteins, and they were determined to be EEFPFA for α2-M and ALKVQTV for PZP, with no interfering sequences detected. The results confirmed the discriminatory capacity of the purification procedure and the purity of the fragments. This new methodology facilitates biological studies of α-macroglobulins, and will enable elucidation of the role the C-terminal region may exert to eliminate α-macroglobulin-proteinases complexes from the circulation by the LRP/receptor. © 2006 Elsevier Inc. All rights reserved.

AB - A new, easier and efficient purification method, using Sephacryl and DEAE-Sephacel, of the C-terminal fragment of two α-macroglobulins, α2-M and PZP, is presented. Two larger peptides were identified for each protein as the C-terminal fragment, with molecular weights of ∼30 kDa and the N-terminal sequences were determined to be SSTQDTV for α2-M and VALHLS for PZP. The smaller peptides with molecular weights of 18 kDa correspond to a shorter C-terminal sequence of these proteins, and they were determined to be EEFPFA for α2-M and ALKVQTV for PZP, with no interfering sequences detected. The results confirmed the discriminatory capacity of the purification procedure and the purity of the fragments. This new methodology facilitates biological studies of α-macroglobulins, and will enable elucidation of the role the C-terminal region may exert to eliminate α-macroglobulin-proteinases complexes from the circulation by the LRP/receptor. © 2006 Elsevier Inc. All rights reserved.

U2 - 10.1016/j.pep.2006.12.008

DO - 10.1016/j.pep.2006.12.008

M3 - Article

SP - 112

EP - 118

JO - Protein Expression and Purification

JF - Protein Expression and Purification

SN - 1046-5928

ER -