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  • Title: Trypanosoma rangeli sialidase lacks trans-sialidase activity.
    Author: Pontes-de-Carvalho LC, Tomlinson S, Nussenzweig V.
    Journal: Mol Biochem Parasitol; 1993 Nov; 62(1):19-25. PubMed ID: 8114822.
    Abstract:
    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 acceptor, no trans-sialidase activity was detected. Nevertheless, T. rangeli lysates and culture supernatants contain a sialidase that hydrolyzes sialyl(alpha 2-3)lactose, and much less efficiently sialyl(alpha 2-6)lactose, but not poly(alpha 2-8)N-acetylneuraminic acid. T. cruzi trans-sialidase hydrolyzed only sialyl(alpha 2-3)lactose under the same conditions. The T. rangeli and the T. cruzi enzymes differ antigenically and in their pH optimum for hydrolase activity.
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