Skip Navigation



Glycobiology Advance Access published online on September 9, 2003
Glycobiology, doi:10.1093/glycob/cwg116
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow All Versions of this Article:
13/12/955    most recent
cwg116v1
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 PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Loganathan, D.
Right arrow Articles by Goldstein, I. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Loganathan, D.
Right arrow Articles by Goldstein, I. J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Submitted on July 31, 2003
Revised on August 26, 2003
Accepted on August 27, 2003

© 2003 Oxford University Press

ORIGINAL ARTICLES

Immobilized Marasmius oreades agglutinin: use for binding and isolation of glycoproteins containing the xenotransplantation or human type B epitopes

Duraikkannu Loganathan 1, Harry C. Winter 1, W. John Judd 2, Jerzy Petryniak 1, and Irwin J. Goldstein 1*

1 Department of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan, 48109-0606
2 Department of Pathology, The University of Michigan Medical School, Ann Arbor, Michigan, 48109-0606

* To whom correspondence should be addressed. E-mail: igoldste{at}umich.edu.

Abstract

The type B-specific lectin from the mushroom Marasmius oreades was immobilized onto Sepharose 4B. The immobilized lectin bound murine laminin and bovine thyroglobulin, glycoproteins that contain the Gal{alpha}1,3Gal{beta}1,4GlcNAc epitope. This epitope is responsible for hyperacute rejection of xenotransplants from lower mammals to humans, old world monkeys, or apes. The immobilized lectin also bound a fraction of serum proteins from type B human serum, but little or none from type A or O(H) serum. The major protein bound from human B serum was a portion of the {alpha}2-macroglobulin. Treatment of this fraction with N-glycosidase F resulted in decreased molecular weight of bands associated with {alpha}2-macroglobulin and loss of their reactivity toward Marasmius oreades lectin. Upon treatment with coffee bean {alpha}-galactosidase, this bound fraction also lost reactivity with Marasmius oreades lectin, but became reactive with Ulex europaeus I lectin, suggesting the presence of L-fucosyl-{alpha}1,2-terminated structures. The presence of blood group epitopes on {alpha}2-macroglobulin has been detected previously by immunological methods, but this is the first isolation and characterization of the specifically-glycosylated fraction of this serum protein. The immobilized lectin also bound a number of proteins from pig, rabbit, and rat serum that were distinct in electrophoretic mobility from the human B-serum components, and presumably contain the xenotransplantation epitope among their glycan structures. This report further demonstrates the utility of immobilized lectins in isolating and characterizing glycan structures of naturally occurring glycoproteins.


Agglutinin, Gal{alpha}1,3Gal{beta}1,4GlcNAc, Marasmius oreades, mushroom lectin, serum glycoproteins
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.