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

A new, easier and efficient purification method, using Sephacryl and DEAE-Sephacel, of the C-terminal fragment of two ?-macroglobulins, ?2-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 se...

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Autores Principales: Barrera, Daniel Iván, Stigbrand, Torgny, Arbeláez, Luis Fernando, Matheus, Luisa
Formato: Artículo (Article)
Lenguaje:Inglés (English)
Publicado: 2007
Materias:
Pzp
Acceso en línea:https://repository.urosario.edu.co/handle/10336/22891
https://doi.org/10.1016/j.pep.2006.12.008
id ir-10336-22891
recordtype dspace
spelling ir-10336-228912022-05-02T12:37:20Z Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from ?-macroglobulins Barrera, Daniel Iván Stigbrand, Torgny Arbeláez, Luis Fernando Matheus, Luisa Alpha 2 macroglobulin Chymotrypsin Low density lipoprotein receptor related protein Monoclonal antibody Peptide fragment Placenta protein Proteinase Unclassified drug Amino acid sequence Article Chemistry Enzyme linked immunosorbent assay Female Human Hydrolysis Isolation and purification Metabolism Molecular genetics Molecular weight Polyacrylamide gel electrophoresis Pregnancy Protein tertiary structure Sequence analysis Time Western blotting Alpha-macroglobulins Amino acid sequence Chymotrypsin Endopeptidases Enzyme-linked immunosorbent assay Female Humans Hydrolysis Ldl-receptor related protein 1 Molecular sequence data Molecular weight Peptide fragments Pregnancy Pregnancy proteins Time factors ?-macroglobulins C-terminal region Chymotrypsin Pzp polyacrylamide gel monoclonal human protein tertiary western Pzp protein Antibodies Blotting Electrophoresis Protein structure Sequence analysis A new, easier and efficient purification method, using Sephacryl and DEAE-Sephacel, of the C-terminal fragment of two ?-macroglobulins, ?2-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 ?2-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 ?2-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 ?-macroglobulins, and will enable elucidation of the role the C-terminal region may exert to eliminate ?-macroglobulin-proteinases complexes from the circulation by the LRP/receptor. © 2006 Elsevier Inc. All rights reserved. 2007 2020-05-25T23:58:35Z info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 10960279 10465928 https://repository.urosario.edu.co/handle/10336/22891 https://doi.org/10.1016/j.pep.2006.12.008 eng info:eu-repo/semantics/openAccess application/pdf instname:Universidad del Rosario
institution EdocUR - Universidad del Rosario
collection DSpace
language Inglés (English)
topic Alpha 2 macroglobulin
Chymotrypsin
Low density lipoprotein receptor related protein
Monoclonal antibody
Peptide fragment
Placenta protein
Proteinase
Unclassified drug
Amino acid sequence
Article
Chemistry
Enzyme linked immunosorbent assay
Female
Human
Hydrolysis
Isolation and purification
Metabolism
Molecular genetics
Molecular weight
Polyacrylamide gel electrophoresis
Pregnancy
Protein tertiary structure
Sequence analysis
Time
Western blotting
Alpha-macroglobulins
Amino acid sequence
Chymotrypsin
Endopeptidases
Enzyme-linked immunosorbent assay
Female
Humans
Hydrolysis
Ldl-receptor related protein 1
Molecular sequence data
Molecular weight
Peptide fragments
Pregnancy
Pregnancy proteins
Time factors
?-macroglobulins
C-terminal region
Chymotrypsin
Pzp
polyacrylamide gel
monoclonal
human
protein
tertiary
western
Pzp protein
Antibodies
Blotting
Electrophoresis
Protein structure
Sequence analysis
spellingShingle Alpha 2 macroglobulin
Chymotrypsin
Low density lipoprotein receptor related protein
Monoclonal antibody
Peptide fragment
Placenta protein
Proteinase
Unclassified drug
Amino acid sequence
Article
Chemistry
Enzyme linked immunosorbent assay
Female
Human
Hydrolysis
Isolation and purification
Metabolism
Molecular genetics
Molecular weight
Polyacrylamide gel electrophoresis
Pregnancy
Protein tertiary structure
Sequence analysis
Time
Western blotting
Alpha-macroglobulins
Amino acid sequence
Chymotrypsin
Endopeptidases
Enzyme-linked immunosorbent assay
Female
Humans
Hydrolysis
Ldl-receptor related protein 1
Molecular sequence data
Molecular weight
Peptide fragments
Pregnancy
Pregnancy proteins
Time factors
?-macroglobulins
C-terminal region
Chymotrypsin
Pzp
polyacrylamide gel
monoclonal
human
protein
tertiary
western
Pzp protein
Antibodies
Blotting
Electrophoresis
Protein structure
Sequence analysis
Barrera, Daniel Iván
Stigbrand, Torgny
Arbeláez, Luis Fernando
Matheus, Luisa
Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from ?-macroglobulins
description A new, easier and efficient purification method, using Sephacryl and DEAE-Sephacel, of the C-terminal fragment of two ?-macroglobulins, ?2-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 ?2-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 ?2-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 ?-macroglobulins, and will enable elucidation of the role the C-terminal region may exert to eliminate ?-macroglobulin-proteinases complexes from the circulation by the LRP/receptor. © 2006 Elsevier Inc. All rights reserved.
format Artículo (Article)
author Barrera, Daniel Iván
Stigbrand, Torgny
Arbeláez, Luis Fernando
Matheus, Luisa
author_facet Barrera, Daniel Iván
Stigbrand, Torgny
Arbeláez, Luis Fernando
Matheus, Luisa
author_sort Barrera, Daniel Iván
title Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from ?-macroglobulins
title_short Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from ?-macroglobulins
title_full Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from ?-macroglobulins
title_fullStr Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from ?-macroglobulins
title_full_unstemmed Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from ?-macroglobulins
title_sort proteolytic hydrolysis and purification of the lrp/alfa-2-macroglobulin receptor domain from ?-macroglobulins
publishDate 2007
url https://repository.urosario.edu.co/handle/10336/22891
https://doi.org/10.1016/j.pep.2006.12.008
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