[Polyacrylamide gel electrophoresis of cellular proteins from parasitic flagellates of the order Trichomonadida]. / Polyacrylamidgel-Elektrophorese zellulärer Proteine von parasitischen Flagellaten der Ordnung Trichomonadida.

Some Trichomonas hominis and Dientamoeba fragilis strains were compared by electrophoretic patterns of total proteins from trophozoites. Easily distinguished patterns divided T. hominis in different types. Significant differences were also seen comparing T. hominis and D. fragilis whilst among strains of D. fragilis electrophoretic protein patterns were mostly found to be accordant.

Electrophoretic analysis of soluble proteins and esterase, superoxide dismutase and acid phosphatase isoenzymes of members of the protozoan family trichomonadidae.

Polyacrylamide gel electrophoresis was used to compare the proteins and isoenzymes of esterase, superoxide dismutase, and acid phosphatase in soluble, whole-cell extracts of four strains of Trichomonas vaginalis, two strains of Trichomonas gallinae, and one strain each of Tritrichomonas foetus, Tritrichomonas augusta, Tetratrichomonas gallinarum, and Pentatrichomonas hominis. Intraspecific, interspecific, and intergeneric differences were found in protein and isoenzyme profiles. At least four to seven isoenzymes were detected among the ten strains for each of the three enzymes studied. Each strain usually contained one or two isoenzymes of both esterase and acid phosphatase, and two or three isoenzymes of superoxide dismutase.

Cell surface carbohydrates in Tritrichomonas foetus.

The cell surface of Tritrichomonas foetus was characterized by using 18 highly purified lectins with specificities for N-acetyl glucosamine, N-acetyl galactosamine, galactose, mannose, and sialic acid. The specificity of the lectin-induced cell agglutination was verified by inhibition of the agglutination with the specific sugars. By using cytochemical techniques associated with electron microscopy, carbohydrates were detected on the cell surface of T. foetus. The following techniques were used: periodic acid--thiosemicarbazide--silver proteinate, concanavalin A--horseradish peroxidase, and ruthenium red. Anionic sites were detected on the cell surface of the protozoan at pH's 1.8 and 7.2 with the use of colloidal iron hydroxide and cationized ferritin particles, respectively. The binding of colloidal iron particles, as well as the agglutination induced by the lectin from Limulus polyphemus, indicated the presence of sialic acid on the cell surface of T. foetus.