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Plant and Cell Physiology, 1986, Vol. 27, No. 2 303-309
© 1986


Article

N-Acetylglucosamine-Containing Glycopeptide Released from Rice Coleoptile Cell Walls by Protease Treatment

Takayuki Hoson1,3 and Shunji Wada2

1Department of Biology, Osaka Kyoiku University Tennoji-ku, Osaka 543, Japan
2Biological Institute, Faculty of Science, Tohoku University Aoba-yama, Sendai 980, Japan

N-Acetylglucosamine-containing glycopeptides were released from the cell walls of rice coleoptiles by treatment with subtilisin. They were purified by successive treatments with different types of proteases and by affinity chromatography using wheat germ lectin- and concanavalin A-Sepharose columns. The glycopeptide finally obtained after gel filtration contained glycine as the N-terminal amino acid and asparagine as the only amino acid capable of linking with the sugar residue. This glycopeptide contained only N-acetylglucosamine and mannose as sugars and could be hydrolyzed by {alpha}-mannosidase and by almond glycopeptidase. It seems to have an oligosaccharide structure, consisting of {alpha} and ß-mannose and chitobiose attached to asparagine. The results indicate that this wall glycopeptide is a component of asparagine-linked glycoprotein.

3Present address: Department of Biology, Faculty of Science, Osaka City University, Sumiyoshi-ku, Osaka 558, Japan.


(Received May 22, 1985; Accepted December 10, 1985)
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