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Expression and purification of a mutant human growth hormone that is resistant to proteolytic cleavage by thrombin, plasmin and human plasma in vitro

Journal of Biotechnology, ISSN: 0168-1656, Vol: 65, Issue: 2, Page: 183-190
1998
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Article Description

The region having a sequence from amino acid 134 to 150 in human growth hormone (hGH) is known to be cleaved by proteases in human plasma, plasmin and thrombin. In this study, oligonucleotide primer-directed mutagenesis was used to produce recombinant mutant hGHs resistant to limited proteolysis by these proteases. Substitution of Arg 134 and Thr 135 of hGH with Asp 134 and Pro 135 yielded a thrombin-resistant hGH mutant, and substitution of Arg 134, Thr 135 and Lys 140 with Asp 134, Pro 135 and Ala 140 yielded a plasmin-resistant hGH mutant. The latter mutant hGH was also insensitive to in vitro proteolysis by human plasma incubated for 7 days. These alterations in amino acid residues of hGH did not disrupt its biological conformation and retained full growth promoting activities on rat Nb2 cells and human T-47D breast cancer cells.

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