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|Title:||Purification and characterization of 31-kDa palm pollen glycoprotein (Ela g Bd 31 K), which is recognized by IgE from palm pollinosis patients||Authors:||Kimura, Y.
Elaeis guineensis Jacq.
Oil palm pollen allergen
|Issue Date:||Apr-2002||Citation:||Kimura, Y.,Maeda, M.,Kimura, M.,Oi, M.L.,Siang, H.T.,Sook, M.H.,Fook, T.C. (2002-04). Purification and characterization of 31-kDa palm pollen glycoprotein (Ela g Bd 31 K), which is recognized by IgE from palm pollinosis patients. Bioscience, Biotechnology and Biochemistry 66 (4) : 820-827. ScholarBank@NUS Repository.||Abstract:||A basic glycoprotein, which was recognized by IgE from oil palm pollinosis patients, has been purified from oil palm pollen (Elaeis guineensis Jacq.), which is a strong allergen and causes severe pollinosis in Malaysia and Singapore. Soluble proteins were extracted from defatted palm pollen with both Tris-HCl buffer (pH 7.8) and Na-acetate buffer (pH 4.0). The allergenic glycoprotein was purified from the total extract to homogeneity with 0.4% yield by a combination of DEAE- and CM-cellulose, SP-HPLC, and gel filtration. The purified oil palm pollen glycoprotein with molecular mass of 31 kDa was recognized by the β1-2 xylose specific antibody, suggesting this basic glycoprotein bears plant complex type N-glycan(s). The palm pollen basic glycoprotein, designated Ela g Bd 31K, was recognized by IgE of palm pollinosis patients, suggesting Ela g Bd 31 K should be one of the palm pollen allergens. The preliminary structural analysis of N-glycans linked to glycoproteins of palm pollens showed that the antigenic N-glycans having α1-3 fucose and β1-2 xylose residues (GlcNAc2-0Man3Xyl 1Fuc1-0GlcNAc2) actually occur on the palm pollen glycoproteins, in addition to the high-mannose type structures (Man 9-5 GlcNAc2).||Source Title:||Bioscience, Biotechnology and Biochemistry||URI:||http://scholarbank.nus.edu.sg/handle/10635/101506||ISSN:||09168451|
|Appears in Collections:||Staff Publications|
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