Production and Characterization of Human Immunodeficiency Virus Integrase Fused with a Maltose-Binding Protein

맥아당결합 단백질에 융합된 면역결핍 바이러스 인테그라제의 생산 및 분석

  • Kim, Do-Jin (College of Industrial Studies, Chung-Ang University) ;
  • Oh, You-Take (College of Industrial Studies, Chung-Ang University) ;
  • Shin, Cha-Gyun (College of Industrial Studies, Chung-Ang University)
  • Published : 1998.02.01

Abstract

Retroviral integrase is required for integration of viral DNA into the host cell chromosome. Human immunodeficiency virus type-1 integrase was partially purified as a part of a fusion protein linked to a maltose-binding protein and characterized in terms of an endonucleolytic activity. The concentration of the fusion protein purified through an amylose column was about 12mg/ml. Indicating that the solubility of the fusion protein is highly increased by the presence of a maltose-binding protein, considering that the integrase protein alone is poorly solubilized. The endonucleolytic activity of the fusion protein was detected at 0.1 to 1.OmM $Mn^{++}$ ion, but not at any concentrations tested of $Mn^{++}$ ion.

Keywords

References

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