A. Razaghi et al., IMMUNODETECTION OF A PROTEIN RELATED TO MAMMALIAN ARRESTIN IN EUGLENA-GRACILIS, Biochemical and biophysical research communications, 233(3), 1997, pp. 601-605
Six monoclonal antibodies directed against different epitopes of bovin
e retinal arrestin recognized a single polypeptide in extracts of achl
orophyllous Euglena gracilis cells. This polypeptide had an apparent m
olecular weight slightly lower: 45kDa vs. 48 kDa, and a more basic iso
electric point compared to that of bovine visual arrestin. It was loca
ted in an insoluble cytoplasmic fraction. Immunofluorescence assays sh
ow a cytoplasmic punctuated pattern suggesting a cluster distribution
or a linkage to some cell structure. The presence of arrestine-like mo
lecules in achlorophyllous Euglena gracilis cells suggests that these
proteins might be involved in a peculiar step of chemical signal trans
duction processes.