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Production, purification and characterization of two recombinant DNA-derived N-terminal ovine growth hormone variants: oGH3 and oGH5
Abstract
chromatography and gel filtration. Both the proteins showed single band on SDS-PAGE and had molecular weight and iso-electric point closer to authentic pituitary GH. The variants oGH3 and oGH5 were compared with the authentic pituitary derived GH in radio immuno assays, radio receptor assays and binding with the monoclonal antibodies OA 11 and OA12.