Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl

Refine search results

Preferences help
enabled [disable] Abstract
Number of results

Results found: 1

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

Search:
in the keywords:  MUCOCYST
help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
Folia Biologica
|
1999
|
vol. 47
|
issue 1-2
61-65
EN
The mucocyst ultrastructure in B. coli has not been described so far. As demonstrated in this work, cytoenzymatic assays on B. coli with the use of a reaction-detecting membrane-coupled hydrolase, i.e., ATP-ase, permitted identification of the mucocysts in the ciliate studied. The shape, size, and location of mucocysts in B. coli trophozoites were found to correspond to descriptions of these structures in other ciliates. The mucocysts were more numerous in B. coli trophozoites isolated from the symptomatic balantidiosis-affected pigs (Group I), and the product of reaction to ATP-ase was more copious than in Group II trophozoites. However, not all the bubble-like structures with similar morphological features reacted positively to the enzyme. The discrepancy was explained by the cytoenzymatic reaction to Beta-GR. The reaction product was visible in the vesicular structures, situated above the plasmolemma, although some of them contained no reaction product. Thus the presence of two types of secretory structure can be inferred: the mucocysts, with ATP-ase in their membranes, and other extrusomes containing active Beta-GR.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.