Journal of South China University of Technology(Natural Science Edition) ›› 2004, Vol. 32 ›› Issue (9): 59-62.

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Isolation, Purification and Structure Analysis of Sweet Potato Glycoprotein

Li Ya- na  Lin Yong- cheng  She Zhi- gang   

  1. Chemistry Postdoctor‚Sun Yat -sen Univ.‚Guangzhou510275‚Guangdong‚China
  • Received:2003-10-21 Online:2004-09-20 Published:2015-09-09
  • Contact: 李亚娜(1975-)‚女‚博士后‚主要从事天然产物方面的研究 E-mail:nayali@sohu.com
  • About author:李亚娜(1975-)‚女‚博士后‚主要从事天然产物方面的研究

Abstract:  By using DEAE-52 cellulose and Sephadex G100 column chromatography‚sweet potato glycoprotein (SPG) was isolated and purified from sweet potato‚and its structure was analyzed including the determination of the purity and molecular mass of SPG by SDS-PAGE‚the identification of the linkage mode of glycopeptide bond by β-erase reaction‚the analysis of monose composition by GLC‚and the deduction of the linkage type of glycosidic bond by IR spectra.The results indicate that SPG is a kind of conjugated protein with covalent bond‚takes on white solid powder and is easily dissolved in water‚with a molecular mass of62ku and an O-linkage.It is also indicated that there areβ-glycosidic bonds and typical amido-carbonyl groups in SPG containing12.01% protein (mass fraction)‚and that SPG saccharide chain is composed of fucose‚arabinose‚mannose‚glucose and galactose.

Key words:  sweet potato glycoprotein, isolation, purification, structure analysis

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