Comparison of 2',3'-cyclic nucleotide 3'-phosphodiesterase and the major component of Wolfgram protein W1.

Wolfgram protein preparations from myelin are heterogeneous mixtures having major components with molecular weights in the 43,000 to 60,000 range. Through the use of an SDS-slab gel electrophoretic system of high resolving power, the Wolfgram 1 (W1) component described by Nussbaum et al. (1977) has been resolved into two components; bovine W1a and W1b proteins are found to have mobilities identical to those of the two 2',3'-cyclic nucleotide 3'-phosphodiesterase (2'3'-CN 3'-ase) components, CNa and CNb (Drummond, 1979). Crossed immunoelectrophoresis with bovine 2',3'-CN 3'-ase demonstrates that CNa and CNb are antigenically indistinguishable. Rat and bovine Wolfgram proteins W1a and W1b, but not the W2 proteins, display cross reactivity with antiserum directed against bovine 2',3'-CN 3'-ase. Chymotryptic and Staphylococcus aureus V8 protease peptide profiles indicate structural similarities between proteins CNa-W1a and CNb-W1b. It is concluded that an inactivated form of 2',3'-Cn 3'-ase is a major component of Wolfgram protein W1. These results are consistent with the studies on the histochemical localization of rat W1 protein by Roussel et al. (1977, 1978).