Method for the isolation of biologically active monomeric immunoglobulin A from a plasma fraction |
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| Authors: | Heinz Leibl Regine Tomasits Hermann M. Wolf Martha M. Eibl Josef W. Mannhalter |
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| Affiliation: | aImmuno AG, Department of Immunological Research, Industriestrasse 131, A-1221 Vienna, Austria;bInstitute of Immunology, University of Vienna, Vienna, Austria |
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| Abstract: | A purification method for immunoglobulin A (IgA) yielding monomeric IgA with a purity of over 97% has been developed. This procedure uses ethanol-precipitated plasma (Cohn fraction III precipitate) as the starting material and includes heparin-Sepharose adsorption, dextran sulfate and ammonium sulfate precipitation, hydroxyapatite chromatography, batch adsorption by an anion-exchange matrix and gel permeation. Additional protein G Sepharose treatment leads to an IgA preparation of greater than 99% purity. The isolated IgA presented with an IgA subclass distribution, equivalent to IgA in unfractionated plasma, and was biologically active, as was shown by its ability to down-modulate Haemophilus influenzae-b-induced IL-6 secretion of human monocytes. |
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| Keywords: | Immunoglobulins |
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