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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)

Abstract

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).

Keywords

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.

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References

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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

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