Comparison of 2′,3′‐Cyclic Nucleotide 3′‐Phosphodiesterase and the Major Component of Wolfgram Protein W1

Abstract

Wolfgram protein preparations from myelin are heterogeneous mixtures having major components with MW ranging from 43,000-60,000. With an SDS-slab gel electrophoretic system of high resolving power the Wolfgram 1 (W1) component described by Nussbaum et al. was resolved into 2 components; bovine W1a and W1b proteins had mobilities identical to those of the two 2'',3''-cyclic nucleotide 3''-phosphodiesterase (2'',3''-CN 3''-ase) components, CNa and CNb (Drummond). Crossed immunoelectrophoresis with bovine 2'',3''-CN 3''-ase demonstrated that CNa and CNb was antigenically indistinguishable. Rat and bovine Wolfgram proteins W1a and W1b, but not the W2 proteins, displayed cross reactivity with antiserum directed against bovine 2'',3''-CN 3''-ase. Chymotryptic and Staphylococcus aureus V8 protease peptide profiles indicated structural similarities between proteins CNa-W1a and CNb-W1b. An inactivated form of 2'',3''-CN 3''-ase apparently is a major component of Wolfgram protein W1.