K
Kenneth W. Talmadge
Researcher at University of Colorado Boulder
Publications - 6
Citations - 1719
Kenneth W. Talmadge is an academic researcher from University of Colorado Boulder. The author has contributed to research in topics: Cell wall & Xyloglucan. The author has an hindex of 6, co-authored 6 publications receiving 1689 citations.
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Journal ArticleDOI
The Structure of Plant Cell Walls: III. A Model of the Walls of Suspension-cultured Sycamore Cells Based on the Interconnections of the Macromolecular Components.
TL;DR: Evidence is provided for a covalent connection between the xyloglucan and pectic polysaccharides and the structural protein of the cell wall and a tentative structure of thecell wall is proposed.
Journal ArticleDOI
The Structure of Plant Cell Walls: I. The Macromolecular Components of the Walls of Suspension-cultured Sycamore Cells with a Detailed Analysis of the Pectic Polysaccharides.
TL;DR: The structures of the pectic polymers (the neutral arabinan, the neutral galactan, and the acidic rhamnogalacturonan) were obtained by methylation analysis of fragments of these polymers which were released from the sycamore walls by the action of a highly purified endopolygalacturonase.
Journal ArticleDOI
The Structure of Plant Cell Walls: II. The Hemicellulose of the Walls of Suspension-cultured Sycamore Cells.
TL;DR: 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 and indicate that xylglucan is covalently linked to the pecticpolysaccharides and is noncovalently bound to the cellulose fibrils of the Sycamore cell wall.
Journal ArticleDOI
Observations on the structure of the phytotoxic glycopeptide of Corynebacterium sepedonicum.
TL;DR: Although the most likely structure of the toxin contains but a single oligosaccharide chain attatched to a single peptide, the evidence suggests that the purest available preparation contains as many ad 5 very similar but not identical glycopeptides.