Vol 64, No 4 (2005)
Original article
Submitted: 2012-02-06
Published online: 2005-09-20
An electron microscopic study of the phosphatases in the ciliate Balantidium coli
Skotarczak B, Kołodziejczyk L
Folia Morphol 2005;64(4):282-286.
Vol 64, No 4 (2005)
ORIGINAL ARTICLES
Submitted: 2012-02-06
Published online: 2005-09-20
Abstract
The localisation and activity of D glucose-6-phosphatase (G-6-Pase) and alkaline
phosphatase (AlP) in the trophozoites of Balantidium coli isolated from pig intestine
content were investigated using ultrastructural and cytochemical methods.
The activity of G-6-Pase was demonstrated on the membranes of the endoplasmic
reticulum, particularly in the cortical part of the trophozoites. In addition, the
product of the reaction to G-6-Pase was concentrated in the vesicular structures,
which were distributed along the reticular membranes. These structures were
described as vesicles similar to glycosomes, containing enzymes of glycogenolysis.
It is very likely that hydrolases in B. coli are formed on the rough reticular membranes
without the involvement of cisterns of the Golgi complex. The ultrastructural
deposits of the reaction to G-6-Pase and AlP in the trophozoites of B. coli
described here indicate that some membranes of the rough endoplasmic reticulum
and small vacuoles with a strong reaction to these enzymes can play a similar
role to the Golgi complex.
Abstract
The localisation and activity of D glucose-6-phosphatase (G-6-Pase) and alkaline
phosphatase (AlP) in the trophozoites of Balantidium coli isolated from pig intestine
content were investigated using ultrastructural and cytochemical methods.
The activity of G-6-Pase was demonstrated on the membranes of the endoplasmic
reticulum, particularly in the cortical part of the trophozoites. In addition, the
product of the reaction to G-6-Pase was concentrated in the vesicular structures,
which were distributed along the reticular membranes. These structures were
described as vesicles similar to glycosomes, containing enzymes of glycogenolysis.
It is very likely that hydrolases in B. coli are formed on the rough reticular membranes
without the involvement of cisterns of the Golgi complex. The ultrastructural
deposits of the reaction to G-6-Pase and AlP in the trophozoites of B. coli
described here indicate that some membranes of the rough endoplasmic reticulum
and small vacuoles with a strong reaction to these enzymes can play a similar
role to the Golgi complex.
Keywords
Ciliata; ultrastructure; phosphatases; cytochemistry
Title
An electron microscopic study of the phosphatases in the ciliate Balantidium coli
Journal
Folia Morphologica
Issue
Vol 64, No 4 (2005)
Article type
Original article
Pages
282-286
Published online
2005-09-20
Page views
498
Article views/downloads
1439
Bibliographic record
Folia Morphol 2005;64(4):282-286.
Keywords
Ciliata
ultrastructure
phosphatases
cytochemistry
Authors
Skotarczak B
Kołodziejczyk L