Production, purification and characterization of two recombinant DNA-derived N-terminal ovine growth hormone variants: oGH3 and oGH5
AbstractTwo recombinant DNA-derived variants of ovine growth hormone were produced, purified, characterized and compared with the authentic pituitary derived GH. The variants oGH3 and oGH5 were isolated by differential centrifugation method and were purified after refolding by ion-exchange
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.