Purification and Some Chemical Properties of 30 kDa Ginkgo biloba Glycoprotein, which Reacts with Antiserum Against β1→2 Xylose-Containing N-Glycans

概要

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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 Man_3Fuc_1Xyl_1GlcNAc_2,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 (Man_3Fuc_1Xyl_1GlcNAc_2)-V-T-V-A-F, which corresponded to the N-terminal amino acid sequence.
社団法人日本農芸化学会の論文
1999-03-23