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.
Turner
J B
JB
Department of Biological Sciences, Manchester Metropolitan University, Manchester, M1 5GD, UK.
Garner
G V
GV
Gordon
D B
DB
Brookes
S J
SJ
Smith
C A
CA
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