Abstract
α-Amylases from germinated maize, oats, rice, and sorghum were isolated by glycogen precipitation and hydrophobic interaction chromatography. Several methods were used for the detection of glycoproteins, including barley α-amylase isozymes purified as previously described and using the rice α-amylase as a positive control for glycosylation. Affinoblotting using concanavalin A, immunoblotting using a xylose-specific serum which reacts with complex N-linked glycans, and endo-β- N-acetylglucosaminidase H treatment of amylases gave negative results for maize, oats, sorghum, and barley. However, after deglycosylation with trifluoromethanesulfonic acid, the molecular weight of one maize α-amylase constituent was clearly decreased. The same result was obtained after β-elimination in mild conditions. Together these results indicated probable O-linked glycosylation of one maize α-amylase when barley, oats, and sorghum α-amylases did not appear to be glycosylated. Chemical deglycosylation of rice α-amylase resulted in the production of two polypeptides with different molecular weights.
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