A novel calcium-independent enzyme capable of incorporating putrescine into proteins.

A Ca(++)-independent enzyme capable of incorporating [3H]-putrescine into proteins was detected in the rat intestine mucosa. The Ca(++)-independent incorporation of [3H]-putrescine into proteins was temperature-, pH-, time-, and dose-dependent. However, this enzyme was absent in the gastric mucosa. Similar to testicular Ca(++)-dependent transglutaminase, the optimal pH of intestinal Ca(++)-independent enzyme was 9.0. At 10(-5) M or less putrescine concentrations, the Ca(++)-independent enzyme in an intestinal cytosol preparation showed a greater activity than did the Ca(++)-dependent transglutaminase. However, at higher putrescine concentrations, the latter showed a greater activity than did the former. Both the intestinal Ca(++)-dependent and independent enzymes were inhibited by cystamine, thermal labile at 50 degrees C and precipitated by 30 to 50% saturation of ammonium sulfate. The fact that these two enzymes shared many similar characteristics, with the exceptions of Ca(++)-requirement, suggests that they may have similar active site and intrinsic molecular function(s).