| Autor: |
Aavo-Valdur Mikelsaar, Gunnar Tasa, Mart Uusküla, Erkki Juronen, Margus Pooga |
| Rok vydání: |
1996 |
| Předmět: |
|
| Zdroj: |
Hybridoma. 15:77-82 |
| ISSN: |
0272-457X |
| Popis: |
The recently discovered human class theta glutathione S-transferase T1-1 (GSTT1-1) is responsible for the GSH-dependent detoxification of naturally occurring monohalomethanes. The detoxifying role of GSTT1-1 has not been investigated in cancer susceptibility and the polymorphism of the protein is unknown in different populations. The purpose of our work was to produce a panel of mouse monoclonal antibodies (MAbs) that could bind to different regions of the GSTT1-1 protein and would help us select suitable MAbs for Western blot analyses and immunohistochemistry, and develop an ELISA assay for detection of GSTT1-1 in whole blood. Six highly specific MAbs were generated against GSTT1-1. Out of six MAbs, one was able to recognize only the native form of the enzyme and possesses two binding sites on the dimeric GSTT1-1 molecule. The other five MAbs bind to both native and denatured GSTT1-1 enzyme in direct and antigen capture ELISA or Western blot. The antibodies recognize at least four different epitopes on the GSTT1-1 molecule. Using MAbs 4G1 and 2D8, a sensitive ELISA assay for determination of GSTT1-1 in whole blood was developed. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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