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.
