DIFFERENCES IN THE NEUROFILAMENT PROTEINS BETWEEN THE PERIKARYON AND AXON OF THE BOVINE SPINAL GANGLION

Perikarya of bovine spinal ganglion cells were dissected out from freeze-dried sections and their neurofilament proteins were analyzed by two-dimensional gel electrophoresis. Neurofilament proteins purified from the bovine spinal cord, a triplet of 76 K, 170 K and 220 K proteins, were used as reference. In the perikarya, the 220 K component was not detected, and the 170 K component was seen in only a trace amount. Instead, a 150 K protein, which was more alkaline than the 170 K component, and a group of proteins ranging from 150 K to 170 K (150-170 K proteins) were dominant in the perikarya. The 150-170 K proteins were also observed in the intraganglionic nerve fibers, in addition to the typical triplet proteins. Immunoblotting with anti-170 K antibody confirmed that the 150 K protein and 150-170 K proteins share the antigenicity with the 170 K protein.