Tandem Mass Spectrometry and Structural Elucidation of Glycopeptides from a Hydroxyproline-rich Plant Cell Wall Glycoprotein Indicate That Contiguous Hydroxyproline Residues Are the Major Sites of Hydroxyproline O-Arabinosylation
Open Access
- 1 February 1995
- journal article
- Published by Elsevier
- Vol. 270 (6) , 2541-2549
- https://doi.org/10.1074/jbc.270.6.2541
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- A (1→3,1→4)‐β‐glucan‐specific monoclonal antibody and its use in the quantitation and immunocytochemical location of (1→3,1→4)‐β‐glucansThe Plant Journal, 1994
- A Histidine-Rich Extensin from Zea mays Is an Arabinogalactan ProteinPlant Physiology, 1992
- A Repetitive Proline-Rich Protein from the Gymnosperm Douglas Fir Is a Hydroxyproline-Rich GlycoproteinPlant Physiology, 1992
- A variable dispersion array detector for a tandem mass spectrometerInternational Journal of Mass Spectrometry and Ion Processes, 1991
- Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltonsAnalytical Chemistry, 1988
- Characterization of Native and Modified Extensin Monomers and Oligomers by Electron Microscopy and Gel FiltrationPlant Physiology, 1988
- Cross-Linking Patterns in Salt-Extractable Extensin from Carrot Cell WallsPlant Physiology, 1986
- Reinforced Polyproline II Conformation in a Hydroxyproline-Rich Cell Wall Glycoprotein from Carrot RootPlant Physiology, 1984
- Arabinogalactan-Proteins: Structure, Biosynthesis, and FunctionAnnual Review of Plant Physiology, 1983
- Cell Surfaces in Plant-Microorganism InteractionsPlant Physiology, 1979