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Monoclonal antibodies were used to study the immunochemical nature of charge isomers of bacterially produced methionyl human growth hormone. After isoelectric focusing of the hormone the 12 monoclonal antibodies reacted similarly in immunoblotting experiments and none of them could discriminate between the two isolated charge isomers in ELISA. This indicates that the generation of charge isomers of met-hGH does not result in loss of the determinants recognized by the monoclonal antibodies and that the conformation of the two main charge isomers is identical within these determinants.
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