A method for efficient and selective recovery of membrane glycoproteins from concanavalin A-Sepharose using media containing sodium dodecyl sulfate and urea

Herpes-specific membrane glycoproteins were recovered from infected cells by incubating total homogenates with Con A-Sepharose in sealed plastic tubes. Following affinity binding of glycoproteins, subsequent washes with media containing high-salt concentrations followed by washes in 0.1% sodium dodecyl sulfate effectively removed nonglycoprotein contaminants. Glycoproteins were then eluted in high yield by heating the Con A-Sepharose-glycoprotein complex in medium containing 5% sodium dodecyl sulfate and 8 m urea. Eluates were placed directly onto sodium dodecyl sulfate-polyacrylamide gels for further analysis and purification of individual components. The procedure described here is convenient for simultaneously processing many different samples on either a large or small scale.