The AMP deaminase activity present in a crude extract of trout gill increased with time. 2. Soybean trypsin inhibitor and alpha2-macroglobulin inhibited the AMP deaminase activation. NEM was also inhibitory at 10-3 M. 3. The activation process is followed by a decrease of activity which is inhibited by EGTA and enhanced by Mg2+. These two compounds were without effect on the activation process itself. 4. Trypsin induces a sharp activation of AMP deaminase in a fresh gill extract but is without effect on a fully activated extract. 5. Overall, the results suggest that neutral proteinases are implicated in AMP deaminase activation.