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).
| Original language | English |
|---|---|
| Pages (from-to) | 820-827 |
| Number of pages | 8 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 66 |
| Issue number | 4 |
| Publication status | Published - Apr 2002 |
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Keywords
- Antigenic N-glycan
- Elaeis guineensis Jacq.
- Oil palm pollen allergen
- Plant glycoprotein
- Pollen allergy
ASJC Scopus subject areas
- Food Science
- Applied Microbiology and Biotechnology
- Chemistry (miscellaneous)
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biotechnology
- Bioengineering
Cite this
Purification and characterization of 31-kDa palm pollen glycoprotein (Ela g Bd 31 K), which is recognized by IgE from palm pollinosis patients. / Kimura, Yoshinobu; Maeda, Megumi; Kimura, Mariko; Oi, Ming Lai; Siang, Hee Tan; Sook, Mei Hon; Fook, Tim Chew.
In: Bioscience, Biotechnology and Biochemistry, Vol. 66, No. 4, 04.2002, p. 820-827.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification and characterization of 31-kDa palm pollen glycoprotein (Ela g Bd 31 K), which is recognized by IgE from palm pollinosis patients
AU - Kimura, Yoshinobu
AU - Maeda, Megumi
AU - Kimura, Mariko
AU - Oi, Ming Lai
AU - Siang, Hee Tan
AU - Sook, Mei Hon
AU - Fook, Tim Chew
PY - 2002/4
Y1 - 2002/4
N2 - 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).
AB - 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).
KW - Antigenic N-glycan
KW - Elaeis guineensis Jacq.
KW - Oil palm pollen allergen
KW - Plant glycoprotein
KW - Pollen allergy
UR - http://www.scopus.com/inward/record.url?scp=0036549833&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036549833&partnerID=8YFLogxK
M3 - Article
C2 - 12036055
AN - SCOPUS:0036549833
VL - 66
SP - 820
EP - 827
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 4
ER -