BIOCHEMICAL CYTOLOGY OF TRICHOMONAD FLAGELLATES
Open Access
- 1 May 1973
- journal article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 57 (2), 453-474
- https://doi.org/10.1083/jcb.57.2.453
Abstract
To determine the localization of several enzymes in Tritrichomonas foetus, the axenic KV-1 strain was grown in Diamond's medium with bovine serum, homogenized in 0.25 M sucrose, and subjected to analytical differential and isopycnic centrifugation. The fractions were assayed for their enzymatic composition and examined electron microscopically. NADH and NADPH dehydrogenases, about 90% of the catalase, and two hydrolases, α-galactosidase and manganese-activated ß-galactosidase I are in the nonsedimentable part of the cytoplasm. α-Glycerophosphate and malate dehydrogenases are associated with a large particle, whose equilibrium density in sucrose gradients is 1.24. This particle corresponds to that population of the paracostal and paraxostylar granules which, having a uniform granular matrix surrounded by a single membrane, resemble microbodies from other organisms. The small sedimentable portion of catalase (about 10% of the total activity) is not associated with these granules and equilibrates at density 1.22. The nature of the subcellular entity carrying catalase could not be ascertained. Hydrolases with a pH optimum around 6–6.5 (protease, ß-N-acetylglucosaminidase, ß-N-acetylgalactosaminidase, and cation-independent ß-galactosidase II), as well as a large part of acid phosphatase, are associated with a population of large particles which equilibrate at densities from 1.15 to 1.20. The hydrolases in these granules lose their structure-bound latency easily after freezing and thawing. These particles correspond to another population of the paracostal and paraxostylar granules which have varied shape and inhomogeneous content with frequent myelin figures, indicating a digestive function. The rest of the phosphatase and most of the acid ß-glucuronidase activity are in a smaller granule fraction with an equilibrium density around 1.18. The latency of these enzymes is quite resistant to freezing and thawing. This particle population consists of smaller, very often flattened vesicles and granules, many of which are clearly fragments of the prominent Golgi apparatus of the cell.Keywords
This publication has 23 references indexed in Scilit:
- Fine structure of chromatic granules inTrichomonas vaginalis DonnéCellular and Molecular Life Sciences, 1970
- Malate dehydrogenase in leaf peroxisomesBiochimica et Biophysica Acta (BBA) - Enzymology, 1969
- THE LARGE-SCALE SEPARATION OF PEROXISOMES, MITOCHONDRIA, AND LYSOSOMES FROM THE LIVERS OF RATS INJECTED WITH TRITON WR-1339The Journal of cell biology, 1968
- DIGESTIVE ACTIVITY OF LYSOSOMES .2. DIGESTION OF MACROMOLECULAR CARBOHYDRATES BY EXTRACTS OF RAT LIVER LYSOSOMES1968
- ELECTRON MICROSCOPIC EXAMINATION OF SUBCELLULAR FRACTIONSThe Journal of cell biology, 1967
- A comparative study of the concrement vacuole of certain endocommensal ciliates—a so-called mechanoreceptorJournal of Ultrastructure Research, 1966
- ELECTRON MICROSCOPIC STUDIES ON PROTOZOAThe Keio Journal of Medicine, 1962
- The Establishment of Various Trichomonads of Animals and Man in Axenic CulturesJournal of Parasitology, 1957
- Tissue fractionation studies. 7. Release of bound hydrolases by means of triton X-100Biochemical Journal, 1956
- Observations on the Trichomonad Flagellate of the Reproductive Organs of CattleJournal of Parasitology, 1951