Abstract
Two 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. Key words: Growth hormone, GH, oGH3, oGH5, radioimmuno assay, radio receptor assay.
Highlights
Growth hormone (GH) is a polypeptide involved in the linear growth of mammals
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
The two N-terminal variants were produced on a large scale by growing E. coli clones carrying plasmid pOGHe103 and pOGHe105 in 500 ml of rich medium containing ampicillin (50 or 100 μg/ml) and IPTG (160 μg/m) at 37oC either shaking for 22 h
Summary
Growth hormone (GH) is a polypeptide involved in the linear growth of mammals. GH is produced by specialized cells in the pituitary gland of mammals, known as somatotrops. The variants oGH3 and oGH5 were isolated by differential centrifugation method and were purified after refolding by ion-exchange chromatography and gel filtration. 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.
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