Abstract:The Trypanosoma rangeli-secreted sialidase was purified by bovine submaxillary gland mucin-sepharose affinity chromatography. In immunoblotting analysis, antibodies raised against this molecule recognized polypeptides of 73 kDa in T. rangeli medium supernatant (TrSialr) and of 70 kDa in the cell lysates of T. rangeli (TrSials) and T. cruzi (TcSialL) epimastigotes. TrSialr, TrSials, and TcSialL were subjected to proteolytic cleavage with papain; the resultant peptide pattern displayed differences in the immunob… Show more
“…In contrast, T. cruzi trans-sialidase transfers sialic residues from the host surface onto mucin molecules on the parasite's surface [3]. Although TrSial has been well characterized [4][5][6][7][8][9], its biological role remains unknown.…”
“…In contrast, T. cruzi trans-sialidase transfers sialic residues from the host surface onto mucin molecules on the parasite's surface [3]. Although TrSial has been well characterized [4][5][6][7][8][9], its biological role remains unknown.…”
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