characterization of purified glutathione s-transferase (gsts) from fasciola hepatica and liver tissue by two-dimensional electrophoresis (2-de)
نویسندگان
چکیده
two-dimensional electrophoresis (2-d electrophoresis) is a powerful and extensively used method for analysis of complex protein mixtures extracted from cells, tissue, or other biological samples such as helminth parasites including, f. hepatica. each spot on the resulting two-dimensional collection corresponds to a single protein species in the sample. this study was carried out to detect of gsts isoenzyme spots map for collection of highly specific proteins. for this purpose, gsts were purified from adult parasite of f.hepatica and sheep liver tissue as an enzyme pool by a glutathione affinity matrix using a wash-bath method and investigated for sodium dodecyl sulphate polyacrylamide gel electrophoresis (sds-page) pattern. for 2-de, purified gsts from f.hepatica and sheep liver tissue were resuspended in sample buffer and then run on a ipg strip in the first dimension and then on an excel gel sds in the second dimension before protein spots staining with coomassie blue. the obtaining spots in the gels were compared and gsts protein spots were detected with similar molecular weight, 26 kda. the protein spots which are recorded in this paper could be gsts isoenzymes and are highly specific peptids. these findings may be considered for vaccination or chemotherapeutic targets in sheep and human fascioliasis.
منابع مشابه
"inhibition assay study of purified glutathione s-transferase from fasciola hepatica and sheep liver tissue by hexachlorophene"
glutathione s-transferases (gsts) are widespread in fasciola. hepatica parasite and sheep liver tissue. study of gsts inhibition assays in f. hepatica and sheep liver tissue are a priority of chemotherapeutic targets in parasitic liver diseases including human fascioliasis in iran. in this research, the whole extract of f. hepatica and sheep liver tissues were purified and eluted for sodium dod...
متن کاملInhibition Assay Study of Purified Glutathione S-transferase from Fasciola Hepatica and Sheep Liver Tissue by Hexachlorophene
Glutathione S-transferases (GSTs) are widespread in Fasciola. hepatica parasite and sheep liver tissue. Study of GSTs inhibition assays in F. hepatica and sheep liver tissue are a priority of chemotherapeutic targets in parasitic liver diseases including human fascioliasis in Iran. In this research, the whole extract of F. hepatica and sheep liver tissues were purified and eluted for sodium dod...
متن کامل"comparative glutathione s-transferases (gsts) inhibition assay in the whole extract of fasciola hepatica and sheep liver tissue by hexachlorophene"
recent research highlights the importance of gsts in the establishment of chronic helminth infections. gsts have the potential to protect the parasite against the host immune response. in this present study, gst enzyme assay has been investigated on whole extract of f. hepatica and sheep liver tissue. to the 1-ml plastic cuvette, added 200 mm potassium phosphate buffer. then added 50 mm gsh red...
متن کاملThe Sigma Class Glutathione Transferase from the Liver Fluke Fasciola hepatica
BACKGROUND Liver fluke infection of livestock causes economic losses of over US$ 3 billion worldwide per annum. The disease is increasing in livestock worldwide and is a re-emerging human disease. There are currently no commercial vaccines, and only one drug with significant efficacy against adult worms and juveniles. A liver fluke vaccine is deemed essential as short-lived chemotherapy, which ...
متن کاملComparative assay of glutathione S-transferase (GSTs) activity of excretory-secretory materials and somatic extract of Fasciola spp parasites.
Fascioliasis is a worldwide parasitic disease in human and domestic animals. The causative agents of fascioliasis are Fasciola hepatica and Fasciola gigantica. In the recent years, fasciola resistance to drugs has been reported in the many of publications. Fasciola spp has detoxification system including GST enzyme which may be responsible for its resistance. Therefore , the aim of the study wa...
متن کاملPurification and characterization of a new cytosolic glutathione S-transferase (glutathione S-transferase X) from rat liver.
A hitherto unknown cytosolic glutathione S-transferase from rat liver was discovered and a method developed for its purification to apparent homogeneity. This enzyme had several properties that distinguished it from other glutathione S-transferases, and it was named glutathione S-transferase X. The purification procedure involved DEAE-cellulose chromatography, (NH4)2SO4 precipitation, affinity ...
متن کاملمنابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
iranian journal of public healthجلد ۳۴، شماره ۲، صفحات ۶۴-۶۷
میزبانی شده توسط پلتفرم ابری doprax.com
copyright © 2015-2023