Glutelin Basic Subunits Have a Mammalian Mucin-Type O-Linked Disaccharide Side Chain

Characterization was done on the sugar chains of glutelin, a major storage protein in rice seeds. The basic subunits of glutelin were shown to be glycoproteins by staining with PAS and the lectins concanavalin A (Con A) and peanut agglutinin (PNA). The binding of PNA to the basic subunits was substa...

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Veröffentlicht in:Archives of biochemistry and biophysics 1999-10, Vol.370 (2), p.271-277
Hauptverfasser: Kishimoto, Tadashi, Watanabe, Mayumi, Mitsui, Toshiaki, Hori, Hidetaka
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Sprache:eng
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Zusammenfassung:Characterization was done on the sugar chains of glutelin, a major storage protein in rice seeds. The basic subunits of glutelin were shown to be glycoproteins by staining with PAS and the lectins concanavalin A (Con A) and peanut agglutinin (PNA). The binding of PNA to the basic subunits was substantially reduced by treatment of the glutelin with NaIO4, NaOH, or O-glycanase. The sugar chains of the subunits, obtained by hydrazinolysis and O-glycanase, were pyridylaminated and subjected to 2-dimensional HPLC analysis using C18 and acrylamide-derivatized columns. It was found that the Galβ-1,3GalNAc disaccharide, which was previously identified as a core 1 structure of mucin-type sugar chains, is conjugated to the glutelin subunits. Furthermore, amino acid sequencing of an 11-kDa peptide of the subunits, recognized by both PNA and Con A, suggested that both N-linked and O-linked glycosylation occurs in the carboxy-terminal region of these subunits.
ISSN:0003-9861
1096-0384
DOI:10.1006/abbi.1999.1406