SDS-polyacrylamide gel electrophoresis was used to characterize labeled proteins transported in rat motor and sensory axons after application of 3H-leucine to the neuron cell bodies. Two types of experiments were performed: first, transported protein accumulating proximal to a ligature placed on the sciatic nerve was analyzed; second, the segment of sciatic nerve nearest to the "wavecrest" of transported protein travelling down the nerve was analyzed. In both cases, no significant differences in peak position or amplitude were found in gels containing labeled proteins from motor or sensory axons. This may mean that the majority of fast-transported protein is involved in an axonal function common to the two types of neuron.

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A previous study revealed a characteristic alteration in the ratio of labeling of two fast axonally transported polypeptides identified as S1 (22,000 daltons) and S2 (18,000 daltons) and their ratio (S2/S1) in rat motoneuron axons following axonal injury and subsequent regeneration. In this study the S2/S1 ratio was determined for axons which were resected and ligated proximally and which did not regenerate to reinnervate muscle. While the initial increase in the S2/S1 ratio following section was the same as that following a crush, the S2/S1 ratio did not return towards normal values after 42 days, but remained elevated for at least 98 days after injury. It is concluded that the return of S2/S1 ratio to normal values, like some other manifestations of the cell body reaction, is delayed if the injured axons do not regenerate.

Axonal transport of labelled protein was studied in rat sciatic nerve by analyzing nerve segments at intervals after injection of L-[3H]leucine into the lumbar spinal cord. Some nerves were sectioned before injection so that material in transit accumulated proximal to the section. The segments distal to the section served as controls for incorporation into the nerve of blood-borne label. An analysis of TCA-soluble and TCA-insoluble activity in cut and intact nerve segments was also made. No evidence was found for the existence of a 'superfast' component of axonal transport (velocity 2000 mm/day). Results showed that the most rapidly transported protein derived from the neuron soma had a conventional 'fast' velocity of 350-420 mm/day. There was no transport of TCA-soluble material. It is suggested that 'superfast' transport, detected in mice by other investigators, is an artefact resulting from failure to control for incorporation of circulating label into the sciatic nerve.

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