Are α-Gliadins Glycosylated?

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.

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