Aminopeptidases of Physarum polycephalum. Activity, isoenzyme pattern, and synthesis during differentiation

In extracts from both growing and differentiating (spherulating) plasmodia of the true slime mold Physarum polycephalum, high aminopeptidase activities were found. The specificity of the aminopeptidases changed during differentiation with a higher relative activity towards hydrophobic NH2-terminal amino acids. This change in specificity was found to be the result of a shift in the isoenzyme spectrum during differentiation as was tested by isoelectric focusing in sucrose gradients. Three different classes of isoenzymes were found: one band which was present in both growing and differentiating cultures; two bands which were found only in growing cultures; and four bands which were detectable only in differentiating plasmodia. If cycloheximide was applied during the induction of differentiation, only one band, the one present in both types of plasmodia, was found in the isoelectric focusing. Density labeling experiments using deuterated amino acids revealed that the bands which are present in differentiated plasmodia only are synthesized de novo during this differentiation.