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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Acceso en línea: | https://repository.urosario.edu.co/handle/10336/22891 https://doi.org/10.1016/j.pep.2006.12.008 |
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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 |
_version_ |
1740172522016473088 |
score |
12,131701 |