Study summary · research use only
Comparison of the antigenicities of native human growth hormone (hGH) and three forms of recombinant hGHs using monoclonal antibodies
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
In this study, a panel of hybridomas producing antibodies against human growth hormone (hGH) was prepared using a recombinant hGH (methionylsomatotropin, r-hGH) as immunogen (host species not stated in the abstract). Thirteen representative monoclonal antibodies were used to analyze the antigenicities of four forms of hGH by RIA inhibition. The abstract reports native hGH and r-hGH showed almost the same antigenicities; a Cys-substituted recombinant hGH (r-hGH-165) retained epitopes recognized by 11 monoclonals but not two; and all but one monoclonal showed little or no reactivity with a recombinant hGH fragment (r-hGH-AB). The authors discuss differences in structure and antigenicity of the recombinant hGH proteins.
Abstract
A panel of hybridomas producing antibodies specific for human growth hormone (hGH) were prepared by using a recombinant hGH [methionylsomatotropin (r-hGH)] as an immunogen. Thirteen representative monoclonal antibodies which showed different reactivity patterns were used to analyze the antigenicities of four different forms of hGHs by RIA inhibition studies. Native hGH and r-hGH showed almost the same antigenicities with these monoclonal antibodies. A Cys-substituted recombinant hGH (r-hGH-165) retained the epitopes recognized by 11 monoclonals but not those recognized by two monoclonals. All except one of the monoclonals showed little or no reactivity with a recombinant hGH fragment (r-hGH-AB). On the basis of these results, the differences in the structures and antigenicities of the recombinant hGH proteins were discussed.
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