Abstract
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.
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References
WARREN, L., AND SPEARING, C.W., (1960) Mammalian Sialidase (Neuraminidase), Biochem. Biophys. Res. Commun. 3, 489–492
CARUBELLI, R., TRUCCO, R.E., AND CAPUTTO, R. (1962) Neuraminidase Activity in Mammalian Organs, Biochim. Biophys. Acta 60, 196–197
ÖHMAN, R., ROSENBERG, A., AND SVENNERHOLM, L. (1970) Human Brain Sialidase, Biochemistry 9, 3774–3782
VENERANDO, B., TETTAMANTI, G., CESTARO, B., AND ZAMBOTTI, V. (1975) Studies on Brain Cytosol Neuraminidase. I. Isolation and Partial Characterization of Two Forms of the Enzyme from Pig Brain, Biochim. Biophys. Acta 403, 461–472
LEIBOVITZ, Z., AND GATT, S. (1968) Enzymatic Hydrolysis of Sphingolipids. VII. Hydrolysis of Gang-liosides by a Neuraminidase from Calf Brain, Biochim. Biophys. Acta 152, 136–143
SVENNERHOLM, L. (1963). Chromatographic Separation of Human Brain Gangliosides, J. Neurochem. 10, 613–623
DRZENIEK, R. (1972) Viral and Bacterial Neuraminidases, in Current Topics in Micro-biology and Immunology, Vol. 59, pp. 35–74, Springer—Verlag, Berlin—Heidelberg—New York
WARREN, L. (1959) The Thiobarbituric Acid Assay of Sialic Acids, J. Biol. Chem. 234, 1971–1975
AMINOFF, D. (1961) Methods for the Quantitative Estimation of N—Acetylneuraminic Acid and their Application to Hydrolysates of Sialomucoids, Biochem. J. 81, 384–392
VEH, R.W., SANDER, M., PARKER, T.L., AND SCHAUER, R. manuscript in preparation
SCHAUER, R., VEH, R.W., WEMBER, M., AND BUSCHER, H.P. (1976) Demonstration of Neuraminidase Activity in Human Blood Serum and Human Milk Using a Modified, Radioactively Labelled a1—Glycoprotein as Substrate, Hoppe—Seyler’s Z. Physiol. Chem. 357, 559–566
VEH, R.W., CORFIELD, A.P., SANDER, M., AND SCHAUER, R. (1977) Neuraminic Acid—Specific Modification and Tritium Labelling of Gangliosides, Biochim. Biophys. Acta 486, 145–160
TALLMAN, J.F., AND BRADY, R.O. (1973) The Purification and Properties of a Mammalian Neuraminidase (Sialidase), Biochim. Biophys. Acta 293, 434–443
BHAVANANDAN, U.P., YEH, A.K., AND CARUBELLI, R. (1975) Neuraminidase Assay Utilizing Sialyl—Oligosaccharide Substrates with Tritium—Labeled Aglycone. Anal. Biochem. 69, 385–394
STRECKER, G., MICHALSKI, J.C., MONTREUIL, J., AND FARRIAUX, J.P. (1976) Deficit in Neuraminidase Associated with Mucolipidosis II (I—Cell Disease), Biomedicine 25, 238–239
SUTTAJIT, M., AND WINZLER, R.J. (1971) Effect of Modification of N—Acetylneuraminic Acid on the Binding of Glycoproteins to Influenza Virus and on Susceptibility to Cleavage by Neuraminidase, J. Biol. Chem. 246, 3398–3404
WALOP, J.N., BOSCHMAN, Th.A.C., AND JACOBS, J. (1960) Affinity of N—Acetylneuraminic Acid for Influenza Virus Neuraminidase, Biochim. Biophys. Acta 44, 185–186
MOHR, E. (1960) Hemmung der Neuraminidase aus Vibrio Cholerae, Z. Naturforsch. 15b, 575–577
GOTTSCHALK, A., AND DRZENIEK, R. (1972) Neuraminidase as a Tool in Structural Analysis, in Glycoproteins, Their Composition, Structure and Function ( Gottschalk, A., Ed.) pp. 381–402, Elsevier Publishing Company, AmsterdamLondon—New York
TETTAMANTI, G., VENERANDO, B., CESTARO, B., AND PRETI, A. (1976) Brain Neuraminidases and Gangliosides, in Ganglioside Function, Biochemical and Pharmacological Implications, ( Porcellati, G., Ceccarelli, B., and Tettamanti, G., eds.), pp. 65–79, Plenum Press, New York and London
HOFSTEE, B.H.J. (1959) Non—Inverted Versus Inverted Plots in Enzyme Kinetics, Nature 184, 1296–1298
TULSIANI, D.R.P., AND CARUBELLI, R. (1970) Studies on the Soluble and Lysosomal Neuraminidases of Rat Liver, J. Biol. Chem. 245, 1821–1827
VISSER, A., AND EMMELOT, P. (1973) Studies on Plasma Membranes. XX. Sialidase in Hepatic Plasma Membranes, 3. Membrane Biol. 14, 73–84
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Veh, R.W., Schauer, R. (1978). Interaction of Human Brain Neuraminidase with Tritium—Labelled Gangliosides. In: Gatt, S., Freysz, L., Mandel, P. (eds) Enzymes of Lipid Metabolism. Advances in Experimental Medicine and Biology, vol 101. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9071-2_41
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DOI: https://doi.org/10.1007/978-1-4615-9071-2_41
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