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A modified gel filtration technique producing an unusual exclusion volume of IgM: a simple way of preparing monoclonal IgM

Authors
Journal
Journal of Immunological Methods
0022-1759
Publisher
Elsevier
Publication Date
Volume
66
Issue
2
Identifiers
DOI: 10.1016/0022-1759(84)90341-7
Keywords
  • Immunoglobulin M Purification
  • Monoclonal Igm
  • Euglobulin
Disciplines
  • Biology

Abstract

Abstract The vast majority of monoclonal IgM proteins is eluted just before the total volume of the column when filtered through G200 Sephadex or S200 Sephacryl gels equilibrated in a 0.005 M phosphate buffer but eluted with 0.05 M phosphate buffer containing 1.7 M NaCl. This unusual behaviour in low-ionic buffer is probably due to the poor solubility of IgM in diluted buffers. It allows a 1-step purification procedure under mild conditions and is suitable for both large and small scale preparations.

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