Plant Physiol. Illumina
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Purification and Characterization of a Galactose-Rich Basic Glycoprotein in Tobacco1

Tetsuo Takeichi*, Junko Takeuchi, Takako Kaneko, and Shinji Kawasaki

National Institute of Agrobiological Resources, Tsukuba, Ibaraki 305, Japan (T.T., S.K.); and Japan Women's University, Faculty of Science II, Bunkyo-ku, Tokyo 112, Japan (J.T., T.K.)

We found a galactose-rich basic glycoprotein (GBGP) in the cell walls of cultured tobacco (Nicotiana tabacum) cells. GBGP and extensin were isolated as the major components of basic, salt-extracted cell wall glycoproteins. GBGP and extensin were separated by gel filtration in 6 m guanidine hydrochloride as 49- and 90-kD peaks, respectively, and further purified with reverse-phase chromatography. The protein moiety of GBGP constitutes about one-half of the molecule (w/w) and contains lysine (16%), proline (12%), hydroxyproline (10%), tyrosine (4%), alanine (7%), leucine (6%), and cystine (1.4%). Galactose accounted for 72% of the sugar moiety, arabinose content was low (17%), and a significant amount of mannose (7%) was found. No immunological cross-reaction was detected between GBGP and extensin. The antibody against native GBGP with sugar chains reacted with other glycoproteins on the gel blots, whereas the antibodies against deglycosylated GBGP and native extensin were highly specific. Immunolocalization analysis in tobacco stems showed that GBGP is specific to parenchyma tissue and that extensin localizes in the epidermis. This tissue-specific and exclusive distribution suggests important functions of these basic glycoproteins.

1   This work was supported by research grants from the Ministry of Agriculture, Forestry, and Fisheries (Tokyo, Japan).
*   Corresponding author; e-mail takeichi{at}abr.affrc.go.jp; fax 81-298-38-8347.

Plant Physiol. (1998) 116: 477-483
Copyright Clearance Center:   0032-0889/98/116/0477/07
© 1998 American Society of Plant Physiologists




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B. H. J. de Graaf, B. A. Knuiman, J. Derksen, and C. Mariani
Characterization and localization of the transmitting tissue-specific PELPIII proteins of Nicotiana tabacum
J. Exp. Bot., January 1, 2003; 54(380): 55 - 63.
[Abstract] [Full Text] [PDF]


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