Abstract
A method is described for the isolation of immunogenically pure IgM from Cohn fraction III of pooled normal plasma by polyethylene glycol precipit ation, delipidation, agar gel chromatography and immuno-adsorption. An S 20.ω 0 of 16·8 and mol. wt of 8942, 000 was determined for monomeric normal IgM. It is postulated that contamination by IgA, IgG an dcomplement components of macromolecular protein solution obtained from Cohn fraction III is caused by soluble complexes. The origins of such complexes are discussed.
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