Abstract
Blix, Gottschalk, and Klenk1 proposed the name ‘neuraminidase’ for the enzyme which splits the glycosidic linkage joining terminal (substituted or unsubstituted) neuraminic acid to residual oligo- or poly-saccharide. Kuhn and Brossmer2 and recently Gottschalk and Graham3 have isolated well-defined substrates by which the enzymatic action of neuraminidase could be studied. There exist many other substrates of high molecular weight and unknown structure; for example, mucoproteins from urine, saliva, serum, or stromata of erythrocytes. Neuraminidase is present in viruses of the myxo-group (influenza, fowl plague, Newcastle disease, mumps) and was found in filtrates of Vibrio cholerae 4 and Clostridium welchii 5.
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References
Blix, F. G., Gottschalk, A., and Klenk, E., Nature, 179, 1088 (1957).
Kuhn, R., and Brossmer, R., Chem. Ber., 89, 2471 (1956); Angewandte Chem., 70, 25 (1958).
Gottschalk, A., and Graham, E. R. B., Z. Naturforsch., 13 b, 821 (1958).
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SCHRAMM, G., MOHR, E. Purification of Neuraminidase from Vibrio cholerae . Nature 183, 1677–1678 (1959). https://doi.org/10.1038/1831677a0
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DOI: https://doi.org/10.1038/1831677a0
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