A novel sialic acid-specific lectin (TFL) was isolated from Tritrichomonas foetus culture supernatant and purified by erythrocyte adsorption followed by fetuin-agarose affinity chromatography. According to gel filtration TFL is a protein of 728 kDa, different from the two sialidases of 853 and 254 kDa, secreted by T. foetus into the medium.
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December 1996
Sialidase, produced by Tritrichomonas mobilensis, a colonic parasite of squirrel monkeys, was purified by adsorption on human RBCs in ice-cold culture supernatant followed by release in PBS at 37 degrees C. The enzyme was purified by size-exclusion chromatography of RBC-eluted material giving a single peak with sialidase activity of molecular weight approx. 630 kDa, representing a quadrimer of the complex of three subunits.
View Article and Find Full Text PDFNew sialic acid-specific lectin has been isolated from culture supernatant of the protozoan Tritrichomonas mobilensis. It was purified by adsorption by erythrocytes or bovine submaxillary gland mucin (BSM)-Sepharose affinity chromatography. The T.
View Article and Find Full Text PDFObjective: To test the dependency of haemolytic and cytocidal manifestations of pathogenicity of Trichomonas vaginalis on direct contact between the target cells and the organism. TEST ORGANISM: T vaginalis strain Baltimore 42.
Design: Haemolysis in the presence of live T vaginalis and of its filter-sterilised metabolic products was compared.
Recently described occurrence of virus-like particles (VLP) in some strains of Trichomonas vaginalis suggests the possibility that the pathogenic significance of this organism may be broadened by its potential for viral transmission. Inasmuch as neither the source nor the host range of the VLP are known, any hazard which they may present for man cannot be estimated. A model has been established for the study of acquisition of known human viruses by T vaginalis.
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