Gel filtration of sialoglycoproteins

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Abstract
The role of sialic acid in the gel-filtration behavior of sialoglycoproteins was investigated using the separated isoenzymes of purified human liver .alpha.-L-fucosidase (EC 3.2.1.51) and several other well-known sialic acid-containing glycoproteins (fetuin, .alpha.1-acid glycoprotein, thyroglobulin and bovine submaxillary mucin). For each glycoprotein studied, gel filtration of its desialylated derivative gave an apparent MW much less than that expected just from removal of sialic acid. For the lower-MW glycoproteins (fetuin and .alpha.1-acid glycoprotein), gel filtration of the sialylated molecules led to apparent MW much larger than the known values. Gel filtration cannot be used for accurately determining the MW of at least some sialoglycoproteins.