RESUMEN
Background: In the recent years, there has been an increasing interest in secretory production of recombinant proteins, due to its various advantages compared with intracellular expression. Signal peptides play a critical role in prosperous secretion of recombinant proteins. Accordingly, different signal peptides have been assessed for their ability to produce secretory proteins by trial-and-error experiments. The aim of this study was to evaluate the effect of L-asparaginase II signal peptide on the recombinant human Growth Hormone [hGH] protein secretion in the Escherichia coli [E. coli] host
Methods: Cloning and expression of a synthetic hGH gene, containing L-asparaginase II signal sequence was performed in E. coli BL21 [DE3] using 0.1mM IPTG as an inducer at 23[degree]C overnight. Periplasmic protein extraction was performed using three methods, including osmotic shock, osmotic shock in the presence of glycine and combined Lysozyme/ EDTA osmotic shock. Afterwards, the hGH expression was determined by SDSPAGE
Results: Based on experimentally obtained results, hGH protein is expressed as inclusion body even in the presence of L-asparaginase II signal peptide
Conclusion: Therefore, this signal peptide is not effective for secretory production of the recombinant hGH