Premium
Immunohistochemical localization of the 150K neurofilament protein in the rat and the rabbit
Author(s) -
Dahl D.,
Bignami A.,
Bich N. T.,
Chi N. H.
Publication year - 1981
Publication title -
journal of comparative neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.855
H-Index - 209
eISSN - 1096-9861
pISSN - 0021-9967
DOI - 10.1002/cne.901950409
Subject(s) - neurofilament , antiserum , biology , protein subunit , spinal cord , anatomy , microbiology and biotechnology , immunohistochemistry , neuroscience , antibody , biochemistry , immunology , gene
Antisera to the 150K‐dalton polypeptide of the bovine neurofilament triplet and chicken neurofilament antisera reacting with the 70K protein in isolated bovine brain filaments stained the same structures in rat cerebellum by immunofluorescence and peroxidase‐antiperoxidase methods, that is Purkinje cell baskets, thin nerve fibers in the lower half of the molecular layer and myelinated axons. The 150K bovine neurofilament antisera did not stain large motor neurons in the anterior horns of the spinal cord in rat and rabbit, nor aluminum‐induced neurofibrillary tangles in the rabbit. All these structures were demonstrated by the chicken neurofilament antisera and by silver neurofibrillary methods. IDPN‐induced axonal balloons containing accumulations of neurofilaments were equally well stained by bovine 150K and chicken neurofilament antisera. These data suggest that the 150K polypeptide of the neurofilament triplet is not a subunit of the neurofilament core and probably plays a role in axonal transport.