PURIFICATION AND CHARACTERIZATION OF ANIONIC TRYPSINS FROM THE HEPATOPANCREAS OF CRAYFISH, PROCAMBARUS-CLARKII

1. Four anionic trypsins, A, B, C, and D, were isolated from crayfish hepatopancreas, and purities were increased 56-, 100-, 87-, and 64-fold with approximately 2.4, 8.1, 5.1, and 3.0% yield, respectively. 2. The molecular weights of trypsin A, B, C, and D were estimated to be 23.8, 27.9, 24.8 and 31.4 kDa, respectively, using Sephacryl S-200 gel filtration. 3. Isoelectric points and amino acid profiles of the four enzymes were similar to other trypsins from marine animals. 4. Thermal stabilities were similar and all were unstable at acidic pH. 5. Sensitivity to inhibitors of these trypsins was similar to trypsin-like enzymes found in marine animals.