Are -Gliadins Glycosylated?

Authors: Turner J.B.; Garner G.V.; Gordon D.B.; Brookes S.J.; Smith C.A.

Source: Protein and Peptide Letters, Volume 9, Number 1, February 2002 , pp. 23-29(7)

Publisher: Bentham Science Publishers

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Abstract:

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

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866023408995

Publication date: 2002-02-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.