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Structure Function Studies of a New World Monkey

α1,3Galactosyltransferase Analysis of Alternative Splicing and Expression in Baculovirus System
  • T. R. Henion
  • U. Galili
Chapter
Part of the Subcellular Biochemistry book series (SCBI, volume 32)

Abstract

The α1, 3galactosyltransferase (α1,3GT) is one of a growing number of cloned glycosyltransferase enzymes which exhibit a remarkable degree of similarity in their overall structure. The α1,3GT, which was simultaneously cloned from the cow (Joziasse et al., 1989) and the mouse (Larsen et al., 1989), was one of the earliest glycosyltransferases for which complete sequence information was available. Since then, over 40 distinct glycosyltransferase genes have been cloned in humans alone. Without exception, each is organized as a type II transmembrane protein, with an N-terminal end within the cytosol and the C-terminal end protruding into the lumen of the endoplasmic reticulum or the Golgi apparatus.

Keywords

Alternative Splice Catalytic Domain World Monkey Stem Region Ehrlich Ascites Tumor Cell 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1999

Authors and Affiliations

  • T. R. Henion
    • 1
  • U. Galili
    • 2
  1. 1.Department of Biomedical SciencesEunice Kennedy Shriver CenterWalthamUSA
  2. 2.Department of Microbiology and ImmunologyMCP-Hahnemann School of MedicinePhiladelphiaUSA

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