Are alpha-gliadins glycosylated?
Alpha-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 alpha-gliadins even after harsh denaturation, but our results indicate alpha-gliadins are not glycoproteins. Suggestions that gliadins are glycoproteins are probably due to contamination with this glucose and the presence of these proteoglycans.
Department of Biological Sciences, Manchester Metropolitan University, Manchester, M1 5GD, UK.
J B
JB
Turner
G V
GV
Garner
D B
DB
Gordon
S J
SJ
Brookes
C A
CA
Smith
D002480:Cellulase; D005903:Gliadin / Q000302:isolation & purification / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism; D006031:Glycosylation; D013058:Mass Spectrometry; D011509:Proteoglycans / Q000737:chemistry / Q000378:metabolism; D014908:Triticum / Q000737:chemistry
D011509:Proteoglycans; D005903:Gliadin; D006026:Glycoside Hydrolases; D002480:Cellulase; C019826:carboxymethylcellulase