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A Sialidase Mutant Displaying trans-Sialidase Activity [PDF]
Journal of Molecular Biology, 2005 Trypanosoma cruzi, the agent of Chagas disease, expresses a modified sialidase, the trans-sialidase, which transfers sialic acid from host glycoconjugates to beta-galactose present in parasite mucins. Another American trypanosome, Trypanosoma rangeli, expresses a homologous protein that has sialidase activity but is devoid of transglycosidase activity.
Gaston Paris, Pedro Alzari
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Trypanosoma rangeli sialidase lacks trans-sialidase activity [PDF]
Molecular and Biochemical Parasitology, 1993 Extracts and tissue culture supernatants of axenic forms of T. rangeli were assayed for the presence of sialidase and trans-sialidase activities. Using sialyl(alpha 2-3)lactose, sialyl(alpha 2-6)lactose, poly(alpha 2-8)N-acetylneuraminic acid, fetuin and 4-methylumbelliferyl-N-acetylneuraminic acid as sialic acid donors, and lactose as a sialic acid ...
Stephen Tomlinson, Víctor Nussenzweig
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Current Protocols in Molecular Biology, 1994
AbstractSialic acids are a family of nine‐carbon acidic sugars found at the nonreducing terminus of many glycoconjugates. Sialidases can remove these sugar units selectively from cell surfaces, membranes, or purified glycoconjugates. In this unit, sialidase digestion of purified glycoproteins is described as is treatment of intact cells.
L D, Powell, A P, Varki
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AbstractSialic acids are a family of nine‐carbon acidic sugars found at the nonreducing terminus of many glycoconjugates. Sialidases can remove these sugar units selectively from cell surfaces, membranes, or purified glycoconjugates. In this unit, sialidase digestion of purified glycoproteins is described as is treatment of intact cells.
L D, Powell, A P, Varki
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Sialidases in biological systems
Die Pharmazie, 2010Sialidases are very common in biological systems. They are found particularly in diverse virus families and bacteria, but also in protozoa, some invertebrates and mammalian. The enzymes differ in their biochemical properties, e.g., kinetics, binding affinity or substrate preference. Nevertheless, they have conserved domains and structural similarities.
Melzig, M. F., Schwerdtfeger, S. M.
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Nature, 1960
THE sialidase of influenza virus has been investigated quantitatively using the method recently described by Warren1 for determining free sialic acid in the presence of the compound bound to muco-protein substrates. For this work, the substrate used was a mucoid derived from the nest-cementing substance of the swiftlet (Collocalia sp.).
C, HOWE, L T, LEE, H M, ROSE
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THE sialidase of influenza virus has been investigated quantitatively using the method recently described by Warren1 for determining free sialic acid in the presence of the compound bound to muco-protein substrates. For this work, the substrate used was a mucoid derived from the nest-cementing substance of the swiftlet (Collocalia sp.).
C, HOWE, L T, LEE, H M, ROSE
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Characterization of myxovirus sialidase
Experientia, 1975Die Sialidasen von Myxoviren zeigten eine ahnliche Substratspezifitat wie die Streptomyces-Sialidase. Siastatin A und B, Produkte von Streptomycesarten, wurden auf ihre hemmende Wirkung gegen Sialidasen verschiedenster Herkunft untersucht und als spezifische Hemmstoffe gegen bakterielle Sialidasen erkannt.
T, Aoyagi +4 more
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Sialidase and malignancy: A minireview
Glycoconjugate Journal, 2003Aberrant sialylation in cancer cells is thought to be a characteristic feature associated with malignant properties including invasiveness and metastatic potential. Sialidase which catalyzes the removal of sialic acid residues from glycoproteins and glycolipids, has been suggested to play important roles in many biological processes through regulation ...
Taeko, Miyagi +3 more
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Structure and Function of Mammalian Sialidases
2012The removal of sialic acids, catalyzed by sialidase, is the initial step in degradation of oligosaccharides, glycoproteins, and glycolipids. The catalytic reaction may greatly influence biological processes through changing the conformation of glycoproteins and create or mask binding sites of functional molecules.
MONTI, Eugenio, Miyagi, Taeko
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Distribution of a novel enzyme of sialidase family among native filamentous fungi
Fungal Biology, 2021Penka Petrova +2 more
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