Are -Gliadins Glycosylated?

Authors: Turner J.B.; Garner G.V.; Gordon D.B.; Brookes S.J.; Smith C.A.

Source: Protein and Peptide Letters, Volume 9, Number 1, February 2002 , pp. 23-29(7)

Publisher: Bentham Science Publishers

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Abstract:

agr -Gliadins isolated by carboxymethylcellulose chromatography contain noncovalently bound glucose probably due to contaminating proteoglycans and to material shed from the column. Traces of carbohydrate remain strongly bound to agr -gliadins even after harsh denaturation, but our results indicate agr -gliadins are not glycoproteins. Suggestions that gliadins are glycoproteins are probably due to contamination with this glucose and the presence of these proteoglycans.

Keywords: Gliadins isolated; carboxymethylcellulose chromatography; Coeliac disease; carboxymethylcellulose CM52; CMC-pooled gliadins; proteoglycan-

Language: English

Document Type: Review article

DOI: 10.2174/0929866023408995

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