Immunodetection of a protein related to mammalian arrestin in Euglena gracilis.
Six monoclonal antibodies directed against different epitopes of bovine retinal arrestin recognized a single polypeptide in extracts of achlorophyllous Euglena gracilis cells. This polypeptide had an apparent molecular weight slightly lower: 45kDa vs. 48 kDa, and a more basic isoelectric point compared to that of bovine visual arrestin. It was located in an insoluble cytoplasmic fraction. Immunofluorescence assays show a cytoplasmic punctuated pattern suggesting a cluster distribution or a linkage to some cell structure. The presence of arrestine-like molecules in achlorophyllous Euglena gracilis cells suggests that these proteins might be involved in a peculiar step of chemical signal transduction processes.
Razaghi
A
A
Laboratoire Métabolisme Cellulaire et Xénobiotiques, Faculté de Pharmacie, Chátenay-Malabry, France.
Bonaly
J
J
Chacun
H
H
Faure
J P
JP
Mirshahi
M
M
Barque
J P
JP
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D019393:Arrestin / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D002417:Cattle; D017124:Conserved Sequence; D003429:Cross Reactions; D000939:Epitopes / Q000737:chemistry / Q000235:genetics; D005056:Euglena gracilis / Q000276:immunology*; D019143:Evolution, Molecular; D015151:Immunoblotting; D007526:Isoelectric Point; D008856:Microscopy, Fluorescence; D008970:Molecular Weight; D015800:Protozoan Proteins / Q000737:chemistry / Q000276:immunology*; D012160:Retina / Q000737:chemistry / Q000276:immunology; D015398:Signal Transduction
D000911:Antibodies, Monoclonal; D019393:Arrestin; D000939:Epitopes; D015800:Protozoan Proteins