<b>Abstract</b>— <p>Basic fibroblast growth factor (FGF-2) is an important regulator of wound healing in humans, which makes it a focus of research in drug and cell therapy development. In this study methods of production, isolation and purification of recombinant human FGF-2 (rhFGF-2) are evaluated and an optimized protocol of rhFGF-2 purification is proposed. Using a <i>Pichia pastoris</i> methylotrophic yeast expression system yield of rhFGF-2 with &gt;98% purity (SDS-PAGE) and high proliferative activity (5.73 ± 2.16 ng/mL) was achieved. The developed approach is suitable for scaling up industrial rhFGF-2 production.</p>

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Optimization of Purification Method of Recombinant Basic Human Fibroblast Growth Factor rhFGF-2 Obtained in Methylotrophic Yeast Pichia pastoris

  • A.-A. V. Misterova,
  • A. S. Gerasimov

摘要

Abstract

Basic fibroblast growth factor (FGF-2) is an important regulator of wound healing in humans, which makes it a focus of research in drug and cell therapy development. In this study methods of production, isolation and purification of recombinant human FGF-2 (rhFGF-2) are evaluated and an optimized protocol of rhFGF-2 purification is proposed. Using a Pichia pastoris methylotrophic yeast expression system yield of rhFGF-2 with >98% purity (SDS-PAGE) and high proliferative activity (5.73 ± 2.16 ng/mL) was achieved. The developed approach is suitable for scaling up industrial rhFGF-2 production.