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5. Involvement of a surface concanavalin A-binding glycoprotein in the adhesion of Trichomonas vaginalis to substrates.

Author

Cappuccinelli, P., Cagliani, Irene, and Cavallo, G.

Abstract

Treatment of Trichomonas vaginalis with EDTA removes their ability to adhere to glass surfaces and changes their affinity to Concanavalin A (ConA) by a different distribution of their surface structures. Filtrates of the EDTA-treated Trichomonas passed through affinity chromatography columns (ConA bound to Sepharose 4B0 separate into 2 fractions, one fraction was bound to the ConA-Sepharose beads, the other was not. The Con A-bound fraction appears to be a glycoprotein which restores in a specific way the ability of the EDTA-treated protozoa to adhere to glass. [ABSTRACT FROM AUTHOR]

Published
1975
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6. Involvement of a surface concanavalin A-binding glycoprotein in the adhesion ofTrichomonas vaginalisto substrates

Author

Cappuccinelli, P., Cagliani, Irene, and Cavallo, G.

Abstract

Treatment ofTrichomonas vaginaliswith EDTA removes their ability to adhere to glass surfaces and changes their affinity to Concanavalin A (ConA) by a different distribution of their surface structures. Filtrates of the EDTA-treatedTrichomonaspassed through affinity chromatography columns (ConA bound to Sepharose 4B0 separate into 2 fractions, one fraction was bound to the ConA-Sepharose beads, the other was not. The Con A-bound fraction appears to be a glycoprotein which restores in a specific way the ability of the EDTA-treated protozoa to adhere to glass.

Published
1975
Full Text
View/download PDF

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