Abstract
Wheat germ agglutinin (WGA) affinity chromatography was examined as a method for the purification of the glycosylated beta subunit from SDS solubilized (Na,K)-ATPase. This lectin, WGA, bound quantitatively all of the beta subunit from SDS solubilized (Na,K)-ATPase whether or not the sample was reduced and/r alkylated. The combination of affinity and high performance size exclusion chromatography purified the beta subunit to a single band on SDS-PAGE electrophoresis. Compared to other methods of isolation this two step procedure utilizing wheat germ agglutinin was superior in terms of yield and purity for the beta subunit of (Na,K)-ATPase.
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