Separation of neurofilaments from ATPase activity by precipitation with anti-neurofilament antibodies.
The possibility that neurofilaments could be involved in the transduction of chemical and mechanical energy in axons led us to investigate whether neurofilament proteins can hydrolyze ATP. We fractionated neurofilaments from rabbit spinal cord and found that preparations highly enriched for neurofilament proteins hydrolyzed ATP at a substantial rate (as high as 0.4 mumol/min/mg protein). However, the ATPase activity was neither inhibited by anti-neurofilament antibody, nor was it precipitated by the antibody under circumstances that precipitated most of the neurofilament polypeptides. We conclude that neurofilament proteins do not hydrolyze ATP at a significant rate under the conditions of our assay; if hydrolysis of ATP is a physiological function of neurofilaments, additional factors are required.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D002458:Cell Fractionation; D003599:Cytoskeleton / Q000648:ultrastructure*; D011817:Rabbits; D013116:Spinal Cord / Q000201:enzymology / Q000648:ultrastructure*; D013347:Subcellular Fractions / Q000201:enzymology
D000906:Antibodies; D000936:Antigen-Antibody Complex; D000251:Adenosine Triphosphatases