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Production and characterization of two monoclonal antibodies to human glutathione peroxidase

H Suemizu1, S Yoshimura, N Tada

  • 1Department of Molecular Life Science (Cell Biology), Tokai University School of Medicine, Isehara-city, Japan.

Hybridoma
|December 1, 1992
PubMed

Glutathione peroxidase (GSH-Px) is an important selenium-containing enzyme which protects cells from oxidative damage. Two hybridoma clones (GPX-121 and GPX-347), producing mouse IgG1 monoclonal antibodies specific for GSH-Px, were established. Immunoblot analysis revealed that GPX-347 was specific for human GSH-Px, while GPX-121 cross-reacted with human, rat, mouse and rabbit GSH-Px. Correlation between GSH-Px content and its enzymatic activity was investigated in erythrocytes of 76 humans and in human lung adenocarcinoma PC-9 cells by using a sandwich type ELISA. The results indicated that GSH-Px activity was expressed higher than expected from GSH-Px content especially in the range of low GSH-Px concentration. PC-9 cells selenium depleted medium did not stain but the cytoplasm of PC-9 cells grown in medium supplemented with selenium stained strongly.

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