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Recombinant human interleukin 2 (rIL-2) enhancement of antibody production by human-human hybridomas
J M McCormack1, M W Cunningham
1Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City 73190.
We studied the effect of highly purified recombinant interleukin 2 from Escherichia coli (rIL-2) on antibody production by our human hybridomas. Increasing concentrations of rIL-2 were directly related to increased production of immunoglobulin, which reached peak levels of 13-25 micrograms/ml, a 10- to 20-fold increase over untreated hybridomas. We were unable to demonstrate large quantities of the IL-2 receptor on the hybridomas as measured by an anti-TAC monoclonal antibody. The data suggest that the antibody enhancement phenomenon is mediated by IL-2 and that is a new, effective way to achieve higher levels of immunoglobulin from human hybridomas.
We studied the effect of highly purified recombinant interleukin 2 from Escherichia coli (rIL-2) on antibody production by our human hybridomas. Increasing concentrations of rIL-2 were directly related to increased production of immunoglobulin, which reached peak levels of 13-25 micrograms/ml, a 10- to 20-fold increase over untreated hybridomas. We were unable to demonstrate large quantities of the IL-2 receptor on the hybridomas as measured by an anti-TAC monoclonal antibody. The data suggest that the antibody enhancement phenomenon is mediated by IL-2 and that is a new, effective way to achieve higher levels of immunoglobulin from human hybridomas.
