Rhus vernicifera laccase (Japanese) was deglycosylated by treating it with exo- and endoglycosidases. In absence of unfolding agents deglycosylation does not exceed 32% while in denaturating conditions only 10% of saccharides are not digested. In the former case specific activity seems to be directly related to the amount of the residual carbohydrates. After deglycosylation in denaturing conditions the modified enzyme exhibits an electrophoretic component of about 60-65 Kd. A stabilizing effect of saccharide moiety on the catalytic site of native laccase was demonstrated. Antiserum raised against the enzyme recognized native Japanese, Vietnamese as well as deglycosylated laccase indicating that the two isoforms are immunologically similar.