Skip Navigation

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 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 arrow Search for citing articles in:
ISI Web of Science (29)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Drake, R. R.
Right arrow Articles by Elbein, A. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Drake, R. R.
Right arrow Articles by Elbein, A. D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology vol 2 no 4 pp. 279-284, 1992
© 1992

review-article

Photoaffinity labelling of glycosyltransferases

Richard R. Drake and Alan D. Elbein

Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Science 4301 West Markham, Little Rock, AR 72205, USA

Received on May 10, 1992; accepted on May 17, 1992

The photoaffinity analogues 5-azido-UDP-glucose and 5-azido-UDP-glucuronic acid have proven to be valuable biochemical tools in the studies of nucleoside diphosphate sugar-utilizing enzymes, especially membrane-associated glycosyltransferases. A summary of the past and current uses of these analogues is presented, as well as photoaffinity data for the enzyme UDP-glucose: dolichylphosphate glucosyltransferase (Glc-P-Dol synthase). This enzyme has served as a model membrane-associated glycosyltransferase for demonstrating the uses of 5-azido-UDP-glucose. The advantages of using photoaffinity analogues for the purification and characterization of glycosyltransferases are presented, as well as an outline of the general procedures which can be used in conjunction with these analogues.

azido-nucleoside diphosphate sugar analogues glycosyltransferases photoaffinity labelling


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
A. Wang-Gillam, I. Pastuszak, M. Stewart, R. R. Drake, and A. D. Elbein
Identification and Modification of the Uridine-binding Site of the UDP-GalNAc (GlcNAc) Pyrophosphorylase
J. Biol. Chem., January 14, 2000; 275(2): 1433 - 1438.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
I. Pastuszak, C. Ketchum, G. Hermanson, E. J. Sjoberg, R. Drake, and A. D. Elbein
GDP-L-fucose Pyrophosphorylase. PURIFICATION, cDNA CLONING, AND PROPERTIES OF THE ENZYME
J. Biol. Chem., November 13, 1998; 273(46): 30165 - 30174.
[Abstract] [Full Text] [PDF]

Home page
 Drug Metab. Dispos.Home page
E. Battaglia, N. Terrier, M. Mizeracka, C. Senay, J. Magdalou, S. Fournel-Gigleux, and A. Radominska-Pandya
Interaction of Periodate-Oxidized UDP-Glucuronic Acid with Recombinant Human Liver UDP-Glucuronosyltransferase 1A6
Drug Metab. Dispos., August 1, 1998; 26(8): 812 - 817.
[Abstract] [Full Text]

Home page
 Drug Metab. Dispos.Home page
E. Battaglia, S. Nowell, R. R. Drake, J. Magdalou, S. Fournel-Gigleux, C. Senay, and A. Radominska
Photoaffinity Labeling Studies of the Human Recombinant UDP-Glucuronosyltransferase, UGT1*6, with 5-Azido-UDP-Glucuronic Acid
Drug Metab. Dispos., April 1, 1997; 25(4): 406 - 411.
[Abstract] [Full Text]

Home page
 Drug Metab. Dispos.Home page
J. M. Little, P. A. Lehman, S. Nowell, V. Samokyszyn, and A. Radominska
Glucuronidation of all-trans-Retinoic Acid and 5,6-Epoxy-all-trans-retinoic Acid. Activation of Rat Liver Microsomal UDP-Glucuronosyltransferase Activity by Alamethicin
Drug Metab. Dispos., January 1, 1997; 25(1): 5 - 11.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
T. Szumilo, Y. Zeng, I. Pastuszak, R. Drake, H. Szumilo, and A. D. Elbein
Purification to Homogeneity and Properties of UDP-GlcNAc (GalNAc) Pyrophosphorylase
J. Biol. Chem., May 31, 1996; 271(22): 13147 - 13154.
[Abstract] [Full Text] [PDF]


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.