Are α-Gliadins Glycosylated?

Author(s): J. B. Turner, G. V. Garner, D. B. Gordon, S. J. Brookes, C. A. Smith

Journal Name: Protein & Peptide Letters

Volume 9 , Issue 1 , 2002


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Abstract:

α-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 α-gliadins even after harsh denaturation, but our results indicate α-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-

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Article Details

VOLUME: 9
ISSUE: 1
Year: 2002
Page: [23 - 29]
Pages: 7
DOI: 10.2174/0929866023408995

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