Production,cross reactivity,and epitope analysis of monoclonal antibodies against rat kidney gamma glutamyltransferase |
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Authors: | Jamal Bayad Nicole Sabolovic Denyse Bagrel Athanase Visvikis Maria Wellman Gerard Siest |
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Affiliation: | (1) Faculté des Sciences Pharmaceutiques et Biologiques, Centre du Médicament, URA CNRS 597, 30, Rue Lionnois, 54000 Nancy, France |
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Abstract: | Eighteen IgGl monoclonal antibodies (blabs) have been produced against gamma-glutamyl transferase (GGT) from rat kidney. They were specific to the light subunit of the enzyme with affinity constants ranging from 0.3 to 7.5 108 M–1, while they did not react with GGT from other sources i.e. human and pig kidney, rat and guinea pig liver, suggesting species and organ specificity. Two of the blabs (N° 11 and 21) lost their immunoreactivities towards rat kidney GGT in the presence of N-acetyl-neuraminic acid, while immunoreactivities of the other blabs were unchanged. Furthermore, Mabs No 11 and 21 did not react with desialylated rat kidney GGT. These findings suggest that N-acetyl-neuraminic acid is involved in the epitopes recognized by these two Mabs.Abbreviations ELISA
enzyme linked immunosorbent assay
- GGT
gamma-glutamyltransferase
- Mab
monoclonal antibody
- SDS-PAGE
sodium dodecyl sulfate-polyacrylamide gel electrophoresis |
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Keywords: | gamma glutamyltransferase glycosylation kidney monoclonal antibodies rat |
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