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PMID: 6197485 Published · ppublish English Journal Article

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

Journal of immunological methods ·Vol. 66 ·No. 2 ·1984-02-10 ·Pages 299-305

Bouvet JP, Pires R, Pillot J

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.

MeSH Terms
Acrylic Resins Antibodies, Monoclonal/isolation & purification Buffers Chromatography, Gel/methods Dextrans Electrophoresis, Polyacrylamide Gel Humans Immunoglobulin M/analysis,isolation & purification Osmolar Concentration
Chemicals
Acrylic Resins Antibodies, Monoclonal Buffers Dextrans Immunoglobulin M Sephacryl Superfine sephadex
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bouvet J P
Pires R
Pillot J
Article Info
Journal
Journal of immunological methods
Abbr.
J Immunol Methods
ISSN
0022-1759
Published
1984-02-10
Pages
299-305
Language
English
Region
Netherlands
NLM ID
1305440
Subset
IM
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