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Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from alpha-macroglobulins.
Umeå University, Faculty of Medicine, Clinical Microbiology. Umeå University, Faculty of Medicine, Clinical Microbiology, Immunology/Immunchemistry.
2007 (English)In: Protein Expression and Purification, ISSN 1046-5928, Vol. 53, no 1, 112-8 p.Article in journal (Refereed) Published
Abstract [en]

A new, easier and efficient purification method, using Sephacryl and DEAE-Sephacel, of the C-terminal fragment of two alpha-macroglobulins, alpha(2)-M and PZP, is presented. Two larger peptides were identified for each protein as the C-terminal fragment, with molecular weights of approximately 30 kDa and the N-terminal sequences were determined to be SSTQDTV for alpha(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 alpha(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 alpha-macroglobulins, and will enable elucidation of the role the C-terminal region may exert to eliminate alpha-macroglobulin-proteinases complexes from the circulation by the LRP/receptor.

Place, publisher, year, edition, pages
2007. Vol. 53, no 1, 112-8 p.
URN: urn:nbn:se:umu:diva-21196DOI: 10.1016/j.pep.2006.12.008PubMedID: 17257854OAI: diva2:210953
Available from: 2009-04-07 Created: 2009-04-07 Last updated: 2009-04-07

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