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-
Protein & Peptide Letters
Title: Are α-Gliadins Glycosylated?
Volume: 9 Issue: 1
Author(s): J. B. Turner, G. V. Garner, D. B. Gordon, S. J. Brookes and C. A. Smith
Affiliation:
Keywords: Gliadins isolated, carboxymethylcellulose chromatography, Coeliac disease, carboxymethylcellulose CM52, CMC-pooled gliadins, proteoglycan-
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.
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Cite this article as:
Turner B. J., Garner V. G., Gordon B. D., Brookes J. S. and Smith A. C., Are α-Gliadins Glycosylated?, Protein & Peptide Letters 2002; 9 (1) . https://dx.doi.org/10.2174/0929866023408995
DOI https://dx.doi.org/10.2174/0929866023408995 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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Protein & Peptide Letters