Sialyltransferases in Young Rat Brain

  • Joel A. Dain
  • Sai-Sun Ng
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 125)


Brain sialyltransferases catalize the transfer of sialic acid (NeuNAc) from CMP-NeuNAc to glycoprotein and glycolipid acceptors. In this study sialyltransferase activities were simultaneously examined utilizing both endogenous and exogenous glycoprotein and glycolipid acceptors. The assumptions were made that the activities obtained with exogenously added substrates are a measure of the amount of sialyltransferases present and that the endogenous activities give additional information on the identity of the endogenous glycoprotein and glycolipid acceptors. Unless otherwise indicated, experiments were performed with a total particulate preparation obtained by centrifuging the homogenate of 11–15 day rat cerebra at 105,000 x g for 1 hr. Four types of sialyltransferase reactions were investigated (A, B, C and D below). Each were assayed by measuring the incorporation (14C)NeuNAc from (14C)-CMP-NeuNAc into a glycolipid or glycoprotein acceptor (NG & DAIN, 1977a,b). The abbreviations for individual gangliosides are those proposed by SVENNERHOLM (1964).


Sialic Acid Chicken Brain Heat Pretreatment Sialyltransferase Activity Sucrose Gradient Fraction 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. KAUFMAN B., BASU S. & ROSEMAN S. (1968): Enzymatic synthesis of disialogangliosides from monosialogangliosides by sialyltransferases from embryonic chicken brain. J. Biol. Chem. 243, 5804–5807.Google Scholar
  2. KEMP S.F. & STOOLMILLER A.C. (1976): Studies on the biosynthesis of glycosphingolipids in cultured mouse neuroblastoma cells. Characterization and acceptor specificities of N-acetylneuraminyl-and N-acetylgalactosaminyltransferases. J. Neurochem. 27, 723–732.PubMedCrossRefGoogle Scholar
  3. MESTRALLET M., CUMAR F.A. & CAPUTTO R. (1977): Trisialoganglioside synthesis by a chicken brain sialyltransferase. Comparative study with the similar reaction for the synthesis of disialoganglioside. Mol. Cell. Biochem. 16, 63–70.Google Scholar
  4. NG S.S. & DAIN J.A. (1977a): Sialyltransferases in rat brain:Reaction kinetics, product analyses, and multiplicities of enzyme species. J. Neurochem. 29, 1075–1083.PubMedCrossRefGoogle Scholar
  5. NG S.S. & DAIN J.A. (1977b): Sialyltransferase in rat brain:Intracellular localization and some membrane properties. J. Neurochem. 29, 1085–1093.PubMedCrossRefGoogle Scholar
  6. SCHACHTER H. & RODEN L. (1973): The biosyntheis of animal glycoproteins, in “Metabolic Conjugation and Metabolic Hydrolysis”, FISHMAN W.H., Eds., Vol. 3, Academic Press (New York and London), pp. 2–149.Google Scholar
  7. SVENNERHOLM L. (1964): The gangliosides. J. Lipid Res. 5, 145–155.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • Joel A. Dain
    • 1
  • Sai-Sun Ng
    • 1
  1. 1.Department of Biochemistry and BiophysicsUniversity of Rhode IslandKingstonUSA

Personalised recommendations