Ultrastructural localization of 28 kDa glutathione S-transferase in adult Clonorchis sinensis
نویسندگان
چکیده
منابع مشابه
Ultrastructural localization of 28 kDa glutathione S-transferase in adult Clonorchis sinensis.
Glutathione S-transferase (28GST) with molecular mass of 28 kDa is an antioxidant enzyme abundant in Clonorchis sinensis. In adult C. sinensis, 28GST was localized in tegumental syncytium, cytons, parenchyma, and sperm tails examined by immunoelectron microscopy. C. sinensis 28GST was earlier found to neutralize bioreactive compounds and to be rich in eggs. Accordingly, it is suggested that 28G...
متن کاملClonorchis sinensis: glutathione S-transferase as a serodiagnostic antigen for detecting IgG and IgE antibodies.
Human Clonorchis sinensis infection is endemic in East Asian countries. Glutathione S-transferases (GSTs) are anti-oxidant enzymes found in all living creatures as well as in trematodes. In this study, we examined the recombinant 26kDa GST protein of C. sinensis (Cs26GST) for its serodiagnostic antigenicity toward IgG and IgE antibodies by ELISA and immuno-enhanced chemiluminescence, respective...
متن کاملTwo glutathione S-transferase inhibitors from Radix Angelicae sinensis.
Chemotherapy for malignant tumors fails because of multidrug resistance (MDR). The overexpression of glutathione S-transferase (GST) with MDR is considered one of the major obstacles to successful cancer chemotherapy. High-throughput screening was performed to search for inhibitors of GST from natural products. Two compounds isolated from Radix Angelicae sinensis had an inhibitory effect on GST...
متن کاملGlutathione-S-transferase variants and adult glioma.
INTRODUCTION Conflicting findings have been reported for associations of primary brain tumors and constitutive polymorphisms in glutathione-S-transferases (GSTs). METHODS We genotyped population-based cases ascertained through rapid case ascertainment and controls identified through random-digit dialing in the San Francisco Bay Area between 1991-1994 (series 1) and 1997-2000 (series 2) for ho...
متن کاملPartial characterization of a 17 kDa protein of Clonorchis sinensis.
A 17 kDa protein from Clonorchis sinensis adults was purified by a procedure including Sephacryl S-200 HR gel filtration and Q-Sepharose anion exchange chromatography. The protein was proved to be a cysteine protease as it showed hydrolytic activity toward Cbz-Phe-Arg-AMC in the presence of dithiothreitol and was inhibited by specific inhibitors such as iodoacetic acid or trans epoxy-succinly-L...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The Korean Journal of Parasitology
سال: 2002
ISSN: 0023-4001
DOI: 10.3347/kjp.2002.40.4.173