Improved Separation at Low Temperature of Glycoproteins by Con A-Sepharose Affinity Chromatography in the Presence of Sodium Dodecyl Sulfate (SDS)
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Abstract
The Con A-Sepharose affinity chromatography of glycoproteins was even more effective at 4 degrees C than that at room temperature (26-28 degrees C) in the presence of sodium dodecyl sulfate (SDS). Application of this methodology to the separation of several glycoproteins from SDS-solubilized membrane proteins in rat cerebellum, including a glycoprotein characteristic of the Purkinje cells, was successful.
Citing Articles
Breen K, Potratz A, Georgopoulou N, Sandhoff K Glycoconj J. 1998; 15(2):199-202.
PMID: 9557882 DOI: 10.1023/a:1006980608983.
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