This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Ryan, C. A. Articles by Albersheim, P. Search for Related Content PubMed PubMed Citation Articles by Ryan, C. A. Articles by Albersheim, P. Agricola Articles by Ryan, C. A. Articles by Albersheim, P.

Articles

A Sycamore Cell Wall Polysaccharide and a Chemically Related Tomato Leaf Polysaccharide Possess Similar Proteinase Inhibitor-Inducing Activities ¹

Alan G. Darvill, Michael McNeil and Peter Albersheim

Institute of Biological Chemistry and Program in Biochemistry and Biophysics, Washington State University, Pullman, Washington 99164, Department of Chemistry, University of Colorado, Boulder, Colorado 80309

A large pectic polysaccharide, called rhamnogalacturonan I, that is solubilized by a fungal endo--1,4-polygalacturonase from the purified walls of suspension-cultured sycamore cells possesses proteinase inhibitor-inducing activity similar to that of the proteinase inhibitor-inducing factor, a pectic-like oligosaccharide fraction isolated from tomato leaves. This suggests that the proteinase inhibitor-inducing activity resides in particular polysaccharide fragments which can be released when plant cell walls are exposed to appropriate enzyme degradation as a result of either wounding or pest attack.

¹ Supported by grants from The Rockefeller Foundation, the National Science Foundation grant PCM 7722195, and the United States Department of Energy grant EY-76-S-02-1426. Scientific Paper No. 5812, Project 1791, College of Agriculture Research Center, Washington State University.

This article has been cited by other articles:

				M. Mutter, I. J. Colquhoun, G. Beldman, H. A. Schols, E. J. Bakx, and A. G.J. Voragen Characterization of Recombinant Rhamnogalacturonan alpha -l-Rhamnopyranosyl-(1,4)-alpha -d-Galactopyranosyluronide Lyase from Aspergillus aculeatus . An Enzyme That Fragments Rhamnogalacturonan I Regions of Pectin Plant Physiology, May 1, 1998; 117(1): 141 - 152. [Abstract] [Full Text]

				M. Mutter, G. Beldman, S. M. Pitson, H. A. Schols, and A. G.J. Voragen Rhamnogalacturonan alpha -d-Galactopyranosyluronohydrolase . An Enzyme That Specifically Removes the Terminal Nonreducing Galacturonosyl Residue in Rhamnogalacturonan Regions of Pectin Plant Physiology, May 1, 1998; 117(1): 153 - 163. [Abstract] [Full Text]

				J. ST. SCHELL Transgenic Plants as Tools to Study the Molecular Organization of Plant Genes Science, September 4, 1987; 237(4819): 1176 - 1183. [Abstract] [PDF]