Dr. Kassai Tibor - Dr. Murai Éva szerk.: Parasitologia Hungarica 10. (Budapest, 1977)
capacity, and roughly identical levels of activity in the other media used (Table 1). Activity was 2-3 times as high in extracts as in nutrient media (Fig. 1). BAEE-hydrolysing (trypsinlike) activity was not demonstrable either in the nutrient media or in extracts. Table 2 Proteolytic activity in parasite extracts Adult: 7; É ; 7. 5; 7; 10; '3; 6; 3. 5; 5; 8; Mean: 6.2 Larvae: 5; 5 ; 7; 5; 5; 1.5; 2. 5; 3. 5; 6; 1; Mean: 4.3 Enzyme activity was recovered by ammonium sulphate fractionation between 40 and 80% saturation. Activity was lost due to denaturation by exposure for 30 minutes at 56°(J, as well as on saturation with 5% TCA (Fig, 1). Addition of 0. 1 ml 0.005% soybean trypsin inhibitor had no influence on enzyme activity. Scrapings of scolex and tegument were tested separately for enzyme activity, but no difference was found from that measured in the whole extract. Protease inhibitors Larvae of L. intestinalis were found to release trypsin and chymotrypsin inhibitors into the nutrient medium (Figs. 1 and 2). Higher inhibitor activities were measured in worm extracts than in culture media of larvae. Table 3 Chymotrypsin-inhibitor activities measured in enzyme-free culture media KRT TS TC 135 TC 199 Tyrode 24 h 48 h 24 h 48 h 24 h 48 h 24 h 48 h 24 h 48 h 4 10 6. 5 13 5 7 6 B 12 20 2 5 6 13 7 8 4 7 13 25 5 7 11 7. 5 4 7 4 5 3 3. 5 6 15 12 12 5 7 3 8 8 8 4 7 10 13 6 8 4 6 7 9 3 6 11 11. 5 2 8 5 9 12 13 Mean: 4 9.1 9.4 11. 6 5 7. 1 4. 3 6. 6 5. 4 13 Table 4 Trypsin-inhibitor activities measured in enzyme-free culture media KRT TS TC 199 Tyrode 24 h 48 h 24 h 48 h 24 h 48 h 24 h 48 h 4. 8 6. 5 1 4. 5 4. 5 7. 5 5 5 9. 5 8. 5 2 4 2 6 3 5 8. 5 12. 0 6 7. 5 1 5. 1 2 3 3. 5 4 5 7 2 7. 5 0 1 6 7. 5 3 3 4 5 4 4 3. 5 5 2. 5 3. 5 3 4 2 4 Mean: 5. 9 5. 5 3. 2 4. 9 2. 7 5. 8 2. 6 3. 6
