Literature DB >> 1421749

Photoaffinity labelling of glycosyltransferases.

R R Drake1, A D Elbein.   

Abstract

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.

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Year:  1992        PMID: 1421749     DOI: 10.1093/glycob/2.4.279

Source DB:  PubMed          Journal:  Glycobiology        ISSN: 0959-6658            Impact factor:   4.313


  2 in total

1.  Purification of a Membrane-Bound UDP-Glucose:Sterol [beta]-D-Glucosyltransferase Based on Its Solubility in Diethyl Ether.

Authors:  D. C. Warnecke; E. Heinz
Journal:  Plant Physiol       Date:  1994-08       Impact factor: 8.340

2.  Identification of endoplasmic reticulum proteins involved in glycan assembly: synthesis and characterization of P3-(4-azidoanilido)uridine 5'-triphosphate, a membrane-topological photoaffinity probe for uridine diphosphate-sugar binding proteins.

Authors:  D M Rancour; A K Menon
Journal:  Biochem J       Date:  1998-08-01       Impact factor: 3.857

  2 in total

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