The effects of S-nitroso-glutathione on the activities of some isoenzymes in Eimeria tenella oocysts

A preliminary study showed that the sporogony process of Eimeria tenella oocysts could be irreversibly inhibited by the S-nitrosothiols, such as S-nitroso-glutathione (GSNO), S-nitroso-N-acetyl-penicillamine. However, the mechanism is unclear at present. In this study the polyacrylamide gel electrophoresis (PAGE) and nitroblue tetrazolium (NBT) photoreduction methods were used to analyze the effects of GSNO on the activities of lactate dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G6PD), aconitase and superoxide dismutase (SOD). Methods of specific substrate staining were employed to display the enzymes after PAGE. The results showed that the activities of LDH, G6PD, aconitase and SOD in fresh unsporulated and sporulated oocysts could be distinctly detected after treatment by GSNO or without treatment. However, there were no obvious alterations of the tested enzymes' activities in all oocysts treated by GSNO or not. This indicated that the inhibitory effects of GSNO on the sporulation of E. tenella oocysts did not work through inactivating the activities of LDH, G6PD, aconitase and SOD, and the activities of these enzymes in sporulated oocysts were also not inactivated by GSNO.