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Are α-Gliadins Glycosylated?

[ Vol. 9 , Issue. 1 ]

Author(s):

J. B. Turner, G. V. Garner, D. B. Gordon, S. J. Brookes and C. A. Smith   Pages 23 - 29 ( 7 )

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-

Affiliation:

Department of Biological Sciences, the Manchester Metropolitan University,Manchester, M1 5GD, UK.



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