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Plant Physiology 51:174-187 (1973)
© 1973 American Society of Plant Biologists

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Articles

The Structure of Plant Cell Walls

II. The Hemicellulose of the Walls of Suspension-cultured Sycamore Cells 1

Wolfgang D. Bauer2, Kenneth W. Talmadge3, Kenneth Keegstra4 and Peter Albersheim5

a Department of Chemistry, University of Colorado, Boulder, Colorado 80302

The molecular structure, chemical properties, and biological function of the xyloglucan polysaccharide isolated from cell walls of suspension-cultured sycamore (Acer pseudoplatanus) cells are described. The sycamore wall xyloglucan is compared to the extracellular xyloglucan secreted by suspension-cultured sycamore cells into their culture medium and is also compared to the seed "amyloid" xyloglucans.

Xyloglucan—or fragments of xyloglucan—and acidic fragments of the pectic polysaccharides are released from endopolygalacturonase-pretreated sycamore walls by treatment of these walls with 8 M urea, endoglucanase, or 0.5 N NaOH. Some of the xyloglucan thus released is found to cochromatograph with the acidic pectic fragments on diethylaminoethyl Sephadex. The chemical or enzymic treatments required for the release of xyloglucan from the walls and the cochromatography of xyloglucan with the acidic pectic fragments indicate that xyloglucan is covalently linked to the pectic polysaccharides and is noncovalently bound to the cellulose fibrils of the sycamore cell wall.

The molecular structure of sycamore xyloglucan was characterized by methylation analysis of the oligosaccharides obtained by endoglucanase treatment of the polymer. The structure of the polymer is based on a repeating heptasaccharide unit which consists of 4 residues of {beta}-1-4-linked glucose and 3 residues of terminal xylose. A single xylose residue is glycosidically linked to carbon 6 of 3 of the glucosyl residues.


2 Present address: MSU/AEC Plant Research Laboratory, Michigan State University, East Lansing, Mich. 48823.

3 National Science Foundation Predoctoral Fellow. Present address: Department of Biology, Princeton University, Princeton, N.J. 08540.

4 National Defense Education Act Predoctoral Fellow. Present address: Room 56-622, Massachusetts Institute of Technology, Cambridge, Mass. 02139.

5 To whom all correspondence should be addressed.

1 Supported in part by Atomic Energy Commission Grant AT(11-1)-1426.




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