Jap. Diniz et M. Benchimol, MONOCERCOMONAS SP - CYTOCHEMISTRY AND FINE-STRUCTURE OF FREEZE-FRACTURED MEMBRANES, The Journal of eukaryotic microbiology, 45(3), 1998, pp. 314-322
Monocercomonas sp. from the wood-snake Tropidophis melanurus was studi
ed using fast freezing of alive and fixed cells followed by freeze-fra
cture and deep-etching. Cytochemistry for enzymes (acid phosphatase, n
eutral phosphatase, and thiaminopyrophosphatase) and for carbohydrates
and endocytosis of gold-labeled albumin were also performed. The Golg
i complex is formed by 12-14 cisternae with typical cis and trans face
s connected to a network of tubular and cisternal structures, and is p
ositive for thiaminopyrophosphatase at the trans face. Intraluminal fi
lamentous structures are seen connecting the two faces of the cisterna
e of the Golgi complex. Lysosomes appeared to contain acid and neutral
phosphatases. Cytochemistry showed that lysosomes predominate among t
he unidentified vacuoles in the cytoplasm. Some vesicles are involved
in the endocytic pathway, while others are derived from the Golgi comp
lex. Hydrogenosomes have a rod-like or dumb-bell shape. Two of the ant
erior flagella present rosettes, when observed in replicas of freeze-f
ractured material, formed by circular arrangement of intramembranous p
articles on both P and E faces. The other anterior and the recurrent f
lagella do not show such rosettes but showed ribbon-like arrays of par
ticles at the point where they emerge from the cell body.