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ATPase Activity in Flagella from Euglena gracilis. Localization of the Enzyme and Effects of Detergents *
Author(s) -
PICCINNI ESTER,
ALBERGONI VINCENZO,
COPPELLOTTI OLIMPIA
Publication year - 1975
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1975.tb05182.x
Subject(s) - flagellum , euglena gracilis , motility , digitonin , atpase , euglena , biology , enzyme , microtubule , v atpase , biophysics , microbiology and biotechnology , biochemistry , chemistry , chloroplast , gene
SYNOPSIS. The biochemical effects of some detergents on the ATPase activity of isolated flagella from Euglena gracilis are related to morphologic obliterations induced by those detergents. Enzymic activity can be localized by electron microscopy along the microtubules and also on the paraflagellar rod. The nonionic detergent digitonin solubilizes the enzyme linked to dyneinic arms, whereas the activity linked to residual structures appears enhanced. These results support the hypothesis that the paraflagellar rod may be a structure actively related to the motility of this type of flagellum.