Rapid purification of immunoglobulin G using aza-arenophilic chromatography: novel mode of protein-solid phase interactions.
A derivative of aza-arenophilic gel having a dichlorosubstituent and an hydroxy ion as a capping nucleophile has been prepared. The properties of this gel in relation to IgG purification have been investigated in details. In the presence of high salt (1.5 M), albumin and some other serum proteins did not bind to the gel. IgG and some other minor proteins, however, were bound to the gel. The bound proteins can be eluted with an acidic buffer. SDS-PAGE showed that the fraction eluted with 0.1 M sodium acetate pH 4.2 consisted mainly of IgGs.
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Department of Developmental and Cell Biology, University of California, Irvine 92717.
D000818:Animals; D001372:Aza Compounds / Q000737:chemistry; D002021:Buffers; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005782:Gels; D006041:Goats; D007074:Immunoglobulin G / Q000302:isolation & purification*; D008024:Ligands; D011506:Proteins / Q000737:chemistry; D011725:Pyridines; D011726:Pyridinium Compounds / Q000737:chemistry
D001372:Aza Compounds; D002021:Buffers; D005782:Gels; D007074:Immunoglobulin G; D008024:Ligands; D011506:Proteins; D011725:Pyridines; D011726:Pyridinium Compounds; C078326:3,5-dichloro-2,4-6-trifluoropyridine