Literature DB >> 2983999

Direct demonstration that the monoclonal antibody AMT-13 and interleukin 2 bind to the same molecule.

H Osawa, T Diamantstein.   

Abstract

125I-labeled surface molecules from mouse T lymphoblasts were fractionated by affinity supports coupled with recombinant interleukin 2 (IL2) and the monoclonal antibody (mAb) AMT-13. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis demonstrated that two molecules of approximately 55 kDa and of approximately 180 kDa were bound in both cases. Sequential precipitation and SDS-PAGE analysis of the precipitated molecules revealed that only the approximately 55-kDa molecule eluted from AMT-13 mAb support was rebound to IL2 affinity support. In addition, IL2 inhibited specifically the binding of 125I-labeled AMT-13 mAb to T lymphoblasts. Thus the results directly demonstrate that the a approximately 55-kDa cell surface molecule represents the IL2-binding protein and that the mAb AMT-13 reacts with this molecule.

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Year:  1985        PMID: 2983999     DOI: 10.1002/eji.1830150317

Source DB:  PubMed          Journal:  Eur J Immunol        ISSN: 0014-2980            Impact factor:   5.532


  3 in total

1.  Cells reacting with the monoclonal anti-IL-2 receptor antibody AMT-13 in the regenerating thymus of irradiated mice.

Authors:  L Takacs; H Osawa; K Liszka; T Diamantstein
Journal:  Clin Exp Immunol       Date:  1986-05       Impact factor: 4.330

2.  Induction of lymphokine-activated killer cells from rat thymocytes using recombinant human interleukin-2.

Authors:  H Imaya; H Matsuura; M Kudo; S Nakazawa
Journal:  Cancer Immunol Immunother       Date:  1988       Impact factor: 6.968

3.  Evaluation of antigen presentation by a murine Ia+ T-cell clone, BK-BI-2.6.C6.

Authors:  A B Reske-Kunz; T Diamantstein
Journal:  Immunology       Date:  1987-08       Impact factor: 7.397

  3 in total

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