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ST3Gal-I

  • Minoru Fukuda
  • Jamey D. Marth

Abstract

ST3Gal-I was originally purified from porcine liver, and the amino acid sequences derived were used for polymerase chain reaction (PCR)-directed cDNA cloning (Gillespie et al. 1992). ST3Gal-I is at present one of six members of the α2,3- sialyltransferase gene family (Ishii et al. 1993; Tsuji et al. 1996; Okajima et al. 1999), and one of the few sialyltransferases that have relatively strict acceptor specificity. Only the corel O-glycan Galβ1→3GalNAc→Ser/Thr can be utilized by ST3Gal-I as an acceptor. The resulting oligosaccharide product is a sialylated corel O-glycan with the structure NeuAcα2→3Galβ1→3GalNAcα1→Ser/Thr, which may also be further sialylated by certain α2,6-sialyltransferases, resulting in a fully sialylated tetrasaccharide: NeuAα2→3Galβ1→3(NeuAα2→6)GalNAcα1→Thr/Ser.

Keywords

Sialic Acid Porcine Liver Peanut Agglutinin Medullary Thymocyte Human Thymic Epithelial 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 Japan 2002

Authors and Affiliations

  • Minoru Fukuda
    • 1
  • Jamey D. Marth
    • 2
  1. 1.Glycobiology ProgramThe Burnham InstituteLa JollaUSA
  2. 2.Howard Hughes Medical InstituteUniversity of California, San DiegoLa JollaUSA

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