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
N1 - Funding Information:
We thank Dr. Per-Ingvar Ohlsson for performing the sequence analysis. This investigation was supported by the Facultad de Ciencias de la Salud, the Vicerrectoría de Investigaciones of Universidad de Pamplona, Pamplona Norte de Santander-Colombia, and the Medical Faculty, University of Umeå Sweden.
Copyright:
Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2007/5
Y1 - 2007/5
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.
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.
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U2 - 10.1016/j.pep.2006.12.008
DO - 10.1016/j.pep.2006.12.008
M3 - Article
C2 - 17257854
AN - SCOPUS:33847163955
SN - 1046-5928
VL - 53
SP - 112
EP - 118
JO - Protein Expression and Purification
JF - Protein Expression and Purification
IS - 1
ER -