Abstract: Two murine monoclonal antibodies specific for IFN‐γ, ADI‐1, and ADI‐23 (both IgG1 kappa), were generated in BALB/c mice. The ADI‐1 exhibited a higher avidity for canine rIFN‐γ than for nIFN‐γ and human rIFN‐γ. In contrast, the ADI‐23 showed equal avidity for the three IFN‐γ preparations. The anti‐canine IFN‐γ mAb did not bind to mouse and rat rIFN‐γ. The ADI‐1, and ADI‐23 mAb were also tested for binding to human rTFN‐α and, contrary to our expectations, it was found that ADI‐23 showed significant binding to human rTFN‐α and rIFN‐γ, in contrast to ADI‐1. Both anti‐canine IFN‐γ mAb stained 48‐h PHA‐induced dog lymphoblasts. A two‐site mAb ELISA was developed, which was linear in the range of 7–500 ng of canine rIFN‐γ, which indicated that the two mAb detected non‐overlapping epitopes on the canine rIFN‐γ molecule. We studied the effect of ADI‐1 on the prolongation of canine renal allografts. Recipients of kidney allografts, that were treated with ADI‐1 by continuous arterial infusion, were prolonged to 22 and 25 days, compared to 9 and 13 days for animals given the IgG1 isotype control.
|Original language||English (US)|
|Number of pages||7|
|State||Published - Mar 1994|
ASJC Scopus subject areas
- Immunology and Allergy