Abstract
The vacuolar/extravacuolar distribution of soluble proteases in Melilotus alba leaf protoplasts has been investigated. The protoplasts were carefully checked and shown to be free of contamination by the proteases of the digestion enzymes. On the basis of substrate specificity pH optima, both endoprotease and exoprotease activities were characterized in protoplasts. However, no carboxypeptidase activity was identified. Aminopeptidases were found to be distributed between the vacuolar and extravacuolar compartments, while the endoproteases were confined to the vacuole.
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