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Purification and Characterization of a Glycine-rich Polypeptide Tightly Bound to Cell Walls from Soybean Aleurone Layers
Abstract:A part of cell walls in soybean aleurone layers remained undigested after pectinase and cellulase treatments, and the features of the undigested cell walls were similar to those of Casparian strips. Glycine-rich polypeptides (GRPP) were extracted with 0.4 n NaOH from the undigested cell walls, Casparian strip-like tissues. Approximately 6.5–kDa GRPP obtained by gel-permeation chromatography from the extract was purified by anion-exchange HPLC and reverse-phase HPLC. The major amino acids of GRPP were glycine (69%) and serine (13%). The n-terminal amino acid sequence of GRPP was the same polyglycine as 30 kDa glycine-rich protein (GRP). GRPP would participate in adhesion between neighboring cells in aleurone layers because of tight binding to the cell wall.
Keywords:glycine-rich polypeptide  aleurone layer  soybean  cell wall  Casparian strip
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