The release of hydrolases from Trichomonas vaginalis and Tritrichomonas foetus.
Trichomonas vaginalis and Tritrichomonas foetus were found to release large amounts of beta-N-acetylglucosaminidase (EC 3.2.1.30), alpha-mannosidase (EC 3.2.1.24), beta-glucosidase (EC 3.2.1.21), acid phosphatase (EC 3.1.3.2) and proteinases during axenic growth in vitro. The enzymes were released continually throughout the growth phase, with the extracellular activity being of the same order as that within the cells. There was differential release of proteinases from Trichomonas vaginalis. The subcellular localization of the hydrolases was determined by differential and isopycnic centrifugation. The intracellular enzymes were shown to be mostly located within particle populations. Centrifugation on Percoll gradients allowed the separation of sub-populations of the particles in T. vaginalis; two distinct sub-populations were apparent with equilibrium densities in 20% (v/v) Percoll of 1.035 and 1.050 g cm-3 respectively. The higher density particles were rich in the hydrolases released most abundantly, suggesting a possible link between enzyme release and these organelles. Distinct subpopulations of hydrolase-containing particles were not detected in Tritrichomonas foetus. The results demonstrate that hydrolytic enzyme release represents a major activity during trichomonad growth.
D000118:Acetylglucosaminidase / Q000378:metabolism; D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D002499:Centrifugation, Density Gradient; D006867:Hydrolases / Q000378:metabolism*; D008361:Mannosidases / Q000378:metabolism; D014246:Trichomonas vaginalis / Q000201:enzymology*; D014318:Tritrichomonas / Q000201:enzymology*; D001617:beta-Glucosidase / Q000378:metabolism
D006867:Hydrolases; D000135:Acid Phosphatase; D008361:Mannosidases; D001617:beta-Glucosidase; D000118:Acetylglucosaminidase