List of Articles Affinity chromatography

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  1 - Purification and Determination of some Characters of Dominant Isoform of GP96 Molecules from Mice Fibrosarcoma Cell Line (WEHI164)
  عقیل Tabar Molla Hassan زهیر Hassan علی Mostafaie سعید Hesaraki علی Taravati
  GP96 protein is a heat shock protein (HSP) with an important role in cellular immunity. Tumorderived gp96 has entered clinical trials for cancer immunotherapy. For purification of dominantisoform of gp96 molecules from mice fibrosarcoma cell line, Cultured WEHI164 cell More

  GP96 protein is a heat shock protein (HSP) with an important role in cellular immunity. Tumorderived gp96 has entered clinical trials for cancer immunotherapy. For purification of dominantisoform of gp96 molecules from mice fibrosarcoma cell line, Cultured WEHI164 cell line werelysed and supernatants of cell extract were precipitated by Amoniume sulfate , In the next stage,purification was done through affinity and ione exchange chromatography. Molecular Weight ofpurified protein was estimated by SDS-PAGE and its nature was confirmed by western blot. Theresult of this study shows that, purified molecule has molecular weight between 66-68 kd whichindicates another different isoform of this molecule; a result confirmed by western blot. Manuscript profile
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  2 - Purification of recombinant human growth hormone produced in soluble form in Escherichia coli in lab-scale
  Seyed Morteza Robatjazi Seyed Mohammad Hasanpour Matikolaee Valiolah Babaeipour Babaeipour Hamideh Rouhani Nejad
  Background & Objectives: Human growth hormone (hGH) or somatotropin is a single chain polypeptide that consisting of 191 amino acid residues and a molecular weight of 22kDa. The purpose of this study was to evaluate the production and purification of the soluble for More

  Background & Objectives: Human growth hormone (hGH) or somatotropin is a single chain polypeptide that consisting of 191 amino acid residues and a molecular weight of 22kDa. The purpose of this study was to evaluate the production and purification of the soluble form of recombinant human growth hormone in the lab-scale.Material & Methods: In this study, the recombinant E. coli containing the plasmid pET32a(+)-hGH was used. To obtain high-level production of soluble hGH in the cytoplasm was used from Trx tag and for the purification process of hGH was used from His tag. The bacteria were grown in LB and TB culture media at 25 ⁰C. The purification process carried out based on affinity chromatography using Ni-NTA resin.Results: The SDS-PAGE analysis showed 55% hGH expression that 33.7% expressed as soluble and 18.8% expressed as IBs. The amount of hGH fusion protein purified through a Ni-NTA column was 22. 4 mg per gram of wet cells.Conclusion: The results of this study indicate that hGH-Trx fusion protein was properly expressed. The purity of hGH fusion protein purified by the histidine-tagged protein purification method was determined by 91% with a total yield of 38%. Manuscript profile