Production of recombinant human apolipoprotein A-I (apoA-I) in E. coli cells is described and its biological properties are compared with those of natural protein. Recombinant apoA-I was isolated as a chimeric polypeptide and then processed to a mature form apoA-I (rapo-I). We studied the ability of the resulting protein to penetrate into hepatocyte nuclei and regulate the rate of DNA biosynthesis in complex with estriol. Penetration of rapoA-I conjugated with FITC into hepatocyte nuclei was demonstrated. rapoA-I–estriol and apoA-I–estriol complexes induced similar increase in DNA biosynthesis rate in isolated hepatocytes, which confi rms functional similarity of the obtained recombinant mature protein (rapoA-I) and native human apoA-I.
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Translated from Kletochnye Tekhnologii v Biologii i Meditsine, No. 3, pp. 155-159, July, 2015
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Ryabchenko, A.V., Kotova, M.V., Tverdohleb, N.V. et al. Production and Analysis of Biological Properties of Recombinant Human Apolipoprotein A-I. Bull Exp Biol Med 160, 129–133 (2015). https://doi.org/10.1007/s10517-015-3113-4
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DOI: https://doi.org/10.1007/s10517-015-3113-4