| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 9607720 | Process Biochemistry | 2005 | 6 Pages |
Abstract
A novel glycoprotein, referred to as WGGP, was isolated from wheat germ water-soluble extracts, and purified by ion-exchange and gel filtration column chromatography. The homogeneity of WGGP was demonstrated by gel filtration on Sepharose CL-6B. The glycoprotein contains 56.4% of protein, rich in glutamic acid, asparagic acid, alanine, glycine, valine and leucine. Mannose accounted for 94% of the neutral sugar moiety, and traces of arabinose, xylose, glucose and galactose were found in WGGP. The molecular weight was estimated to be about 40,000 on SDS-PAGE. The existence of O-glycosidic linkage in WGGP was demonstrated with a β-elimination reaction.
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Authors
Kexue Zhu, Huiming Zhou,