Characterization of an active hydrophilic erythrocyte membrane acetylcholinesterase obtained by limited proteolysis of the purified enzyme.

Purified human erythrocyte membrane acetylcholinesterase was subjected to limited proteolysis with papain. This treatment generated a hydrophilic form of the enzyme as determined by charge-shift crossed immunoelectrophoresis and by binding to phenyl-Sepharose. The hydrophilic enzyme was stable and its activity was independent of the presence of amphiphiles. Electroimmunochemical analysis showed no antigenic difference between the two enzyme forms. Although the proteolytic treatment only brought about a small change in molecular weight, marked differences in the hydrodynamic properties were encountered. The Stokes radius decreased from 8.2 to 5.9 nm and the sedimentation coefficient increased from 6.3 to 7.0 S. The results are consistent with the view that a short hydrophobic peptide responsible for the amphipatic character of acetylcholinesterase is removed by the treatment with papain.