Interaction of Human Brain Neuraminidase with Tritium—Labelled Gangliosides

  • R. W. Veh
  • R. Schauer
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 101)


Since the first demonstration of neuraminidase activity in mammals (1,2), the brain was recognised as a major source of this enzyme. In this organ soluble activity could be detected (3,4), however in most species the bulk of the enzyme proved to be membrane-bound. The first detailed description of a mammalian brain neuraminidase was given by Leibovitz and Gatt (5). Working with calf brain these investigators were able to solubilise about 30% of the neuraminidase activity by sequential treatment with sodium cholate and Triton X-100, and they obtained by this procedure an enzyme preparation purified sixfold over the starting material. Attempts to further purify the enzyme were unsuccessful. A modification of this method has been used in a detailed study of the neuraminidase present in human brain by Öhman et al. (3), but also in this case no further purification could be achieved.


Galacturonic Acid Sodium Cholate Neuraminic Acid Prolonged Incubation Time Neuraminidase Activity 
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Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • R. W. Veh
    • 1
  • R. Schauer
    • 1
  1. 1.Institut für Physiologische ChemieRuhr-Universität BochumBochum 1Germany

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