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KMID : 0370219980420010046
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Yakhak Hoeji
1998 Volume.42 No. 1 p.46 ~ p.52
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Production and Characterization of Human Immunodeficiency Virus Integrase Fused with a Maltose-Binding Protein
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김도진/Kim DJ
오유택/신차균/Oh YT/Shin CG
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Abstract
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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 Mg++ ion.
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