Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 15

Liczba wyników na stronie
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników

Wyniki wyszukiwania

help Sortuj według:

help Ogranicz wyniki do:
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
The activity of aspartate (AsAT) and alanine (A1AT) aminotransferases was examined in liver, head kidney, excretory kidney and sppleen of the carp (Ciprinus carpio L.) with erythrodermatitis. In all the organs studies except liver a general decrease in the activity of both aminotransferases was found as compared with their activity in tissues of healthy fish. This may reflect a disfunction of those organs as a result of a long-lasting effect of the pathogenic factor.
Antioxidant enzymes: catalase (CAT) [EC 1.11.1.6], peroxidase [EC 1.11.1.7], glutathione reductase (GSSGR) [EC 1.6.4.2] and glucose-6-phosphate dehydrogenase (G6PDH) [EC 1.1.1.49] were investigated in terrestrial Helix aspersa (O.F. Müll.) and aquatic Pomacea bridgesi (Reeve). The activity was determined in the heamolymph and homogenates of hepatopancreas and foot muscle. No CAT and peroxidase activity was detected in the hepatopancreas and foot muscle of P. bridgesi, and its haemolymph displayed a very low CAT activity (0.005 U/mg of protein). In H. aspersa the highest activities (U/g) observed for CAT and GSSGR in the hepatopancreas were 0.40, and 1.05, respectively; for peroxidase and G6PDH in the foot muscle the respective values were 1.22 and 0.22. The activities of antioxidant enzymes determined in both snail species are much lower than the corresponding values for mammalian tissues.
Key enzymes of gluconeogenesis, D-glucose-6-phosphatase (G-6-Pase) [EC 3.1.3.9] and D-fructose-1,6-bisphosphate 1-phosphohydrolase (Fru-1,6-Pase) [EC 3.1.3.11], were investigated in Helix pomatia L. and Pomacea bridgesii (Reeve). Fru-1,6-Pase and G-6-Pase activities were determined measuring with malachite green the concentration of inorganic phosphate produced by substrate hydrolysis in homogenates of hepatopancreas, kidney and foot muscle. Determined Fru- , -Pase activities (U/g wt.) in H. pomatia were as follows: hepatopancreas 1.01, kidney 0.19, foot muscle 0.24, in P. bridgesii the respective values were: 0.94, 0.34 and 0.22. Activities of G-6-Pase (U/g wt.) in H. pomatia were: 1.65 in hepatopancreas, 0.64 in kidney and 0.21 in foot muscle, in P. bridgesii the respective values were: 0.79, 0.31, 0.21. Thus the highest gluconeogenic capacity in both species was found in hepatopancreas. Fru-1,6-Pase from H. pomatia and P. bridgesii hepatopancreas was inhibited by AMP. Determined I0.5 were 8.4 M for H. pomatia and 7.3 M for P. bridgesii, and the values were comparable with those of mammalian liver Fru-1,6-Pase. Km determined for hepatopancreas G-6-Pase from H. pomatia and P. bridgesii were 1.3 mM and 4.1 mM, respectively and were also comparable with Km of mammalian liver enzyme.
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.