Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (25)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wojtaszek, P.
Right arrow Articles by Bolwell, G. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wojtaszek, P.
Right arrow Articles by Bolwell, G. P.
Agricola
Right arrow Articles by Wojtaszek, P.
Right arrow Articles by Bolwell, G. P.

PLANT PHYSIOLOGY , Vol 108, Issue 3 1001-1012, Copyright © 1995 by American Society of Plant Biologists


DEVELOPMENT AND GROWTH REGULATION

Secondary Cell-Wall-Specific Glycoprotein(s) from French Bean Hypocotyls

P. Wojtaszek and G. P. Bolwell
Division of Biochemistry, School of Biological Sciences, Royal Holloway and Bedford New College, University of London, Egham, Surrey TW20 0EX, United Kingdom

Specific labeling of secondary cell walls of tracheary elements and of xylary and phloem fibers has been observed when wheat germ agglutinin (WGA) and anti-WGA antibodies were used during ultrastructural studies of French bean (Phaseolus vulgaris L.) hypocotyls. In this report we demonstrate that at least part of this labeling is due to the presence of secondary cell-wall-specific glycoproteins. Three major novel glycoproteins with relative molecular weights of 55,000, 86,000, and 90,000, purified by means of WGA-Sepharose affinity chromatography, have been characterized. Their amino acid composition indicates that they are not the members of known classes of structural cell-wall proteins, since they contain no hydroxyproline, a lower level of glycine than seen in glycine-rich proteins, and very little proline. N-terminal sequences of all three proteins show no significant homology with other proteins. Antibodies were raised against electrophoretically pure 90-kD glycoprotein. These were used to localize this protein in secondary cell walls of xylem tracheary elements and in xylary and phloem fibers, i.e. in the same compartments where labeling with WGA has been observed. To our knowledge this is one of the first biochemical and ultrastructural demonstrations of secondary cell-wall-specific glycoproteins.


This article has been cited by other articles:


Home page
J. Cell Sci.Home page
K Schmidt, H Dartsch, D Linder, H. Kern, and R Kleene
A submembranous matrix of proteoglycans on zymogen granule membranes is involved in granule formation in rat pancreatic acinar cells
J. Cell Sci., January 6, 2000; 113(12): 2233 - 2242.
[Abstract] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1995 by the American Society of Plant Biologists