Abstract
From the seeds of Ginkgo biloba, a glycoprotein, which is a major component that reacts with an antiserum against β1→2 xylose-containing N-glycans, has been purified and characterized. The N-terminal amino acid sequence of the purified glycoprotein was H-K-A-N-X-V-T-V-A-F-V-M-T-Q-H-L-L-F-G-Q-. The molecular mass was estimated to be 17 kDa and 16 kDa by SDS-PAGE under reducing conditions, however, the molecular mass of this glycoprotein in the native state was 30,762 by MALDI-TOF MS, suggesting that this glycoprotein consists of two subunits; one is glycosylated and the other is not. The structure of N-glycan linked to this glycoprotein (designated 30 kDa GBGP) was identified as Man3Fuc1Xyl1GlcNAc2, which is the predominant N-glycan linked to the storage glycoproteins in the same seeds (Kimura, Y et al. (1998) Biosci. Biotechnol. Biochem. 62, 253-261). From the peptic digest of the carboxymethylated glycosylated subunit, one glycopeptide was purified by RP-HPLC and the amino acid sequence was identified as H-K-A-N-N(Man3Fuc1Xyl1GlcNAc2)-V-T-V-A-F, which corresponded to the N-terminal amino acid sequence.
Original language | English |
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Pages (from-to) | 463-467 |
Number of pages | 5 |
Journal | Bioscience, Biotechnology and Biochemistry |
Volume | 63 |
Issue number | 3 |
DOIs | |
Publication status | Published - Jan 1 1999 |
Keywords
- Antigenic N-glycan
- Antiserum against plant N-glycan
- Ginkgo biloba
- Immunoblotting
- Plant glycoprotein
ASJC Scopus subject areas
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry