A method for efficient and selective recovery of membrane glycoproteins from concanavalin A-Sepharose using media containing sodium dodecyl sulfate and urea
✍ Scribed by Laurent Poliquin; Gordon C. Shore
- Publisher
- Elsevier Science
- Year
- 1980
- Tongue
- English
- Weight
- 564 KB
- Volume
- 109
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
✦ Synopsis
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.