| Autor: |
Solovyev MM; Institute of Systematics and Ecology of Animals, Siberian Branch of RAS, Frunze Street, 11, Novosibirsk, Russia, 630091. yarmak85@mail.ru.; Tomsk State University, Tomsk, Russia, 634050. yarmak85@mail.ru., Kashinskaya EN; Institute of Systematics and Ecology of Animals, Siberian Branch of RAS, Frunze Street, 11, Novosibirsk, Russia, 630091., Rogozhin EA; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, GSP-7, Miklukho-Maklaya Street, 16/1, Moscow, Russia, 117997.; Institute of Ecological and Agricultural Biology (X-Bio), Tyumen State University, Volodarskogo Street, 6, Tyumen, Russia, 625003., Moyano FJ; Departamento de Biología y Geología, Facultad de Ciencias, Campus de Excelencia Internacional del Mar (CEI-MAR), Universidad de Almería, La Cañada de San Urbano, 04120, Almería, Spain. |
| Abstrakt: |
The objective of the present study was to assess if trypsin, a key enzyme involved in protein digestion, presents some kind of functional adaptations to seasonal changes in water temperature in freshwater fish. In order to test this hypothesis, individuals of two fish species Carassius gibelio (agastric) and Perca fluviatilis (gastric) were sampled in the basin of Chany Lake (Siberia, Russia) at two different seasons (spring and summer). Apparent kinetic parameters (K m and V max ) were determined for both species and seasons at the actual pH values in fish guts, and at actual temperatures. Results showed a significant effect of both the species and sampling season on the apparent kinetic parameters of trypsin. In the case of Prussian carp, K m and V max were lower for each assayed temperature (for 5 and 15 °C the differences were significant) for fish sampled in summer when compared to those sampled in spring. In contrast, values of K m in perch tended to be lower in spring at 5 and 25 °C but these differences were not significant, while V max showed a significant decrease in summer samples. This suggests a sort of functional adaptation of the same trypsin enzymes to seasonal changes, oriented to maximize protein digestion under variable conditions. |
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