Synthesis in Escherichia coli and Characterization of Human Recombinant Erythropoietin with Additional Heparin-Binding Domain

@article{Karyagina2018SynthesisIE,
  title={Synthesis in Escherichia coli and Characterization of Human Recombinant Erythropoietin with Additional Heparin-Binding Domain},
  author={Anna S. Karyagina and Tatyana M. Grunina and M. S. Poponova and P. A. Orlova and Vasily N Manskikh and Aleksandr Demidenko and N. V. Strukova and M. S. Manukhina and Kirill Nikitin and Alexander M. Lyaschuk and Zoya M. Galushkina and S. A. Cherepushkin and Nikita B Polyakov and Aleksey I Solovyev and Vladimir G. Zhukhovitsky and D. A. Tretyak and Irina S. Boksha and Alexey V. Gromov and Vladimir G. Lunin},
  journal={Biochemistry (Moscow)},
  year={2018},
  volume={83},
  pages={1207-1221}
}
Recombinant human erythropoietin (EPO) with additional N-terminal heparin-binding protein domain (HBD) from bone morphogenetic protein 2 was synthesized in Escherichia coli cells. A procedure for HBD-EPO purification and refolding was developed for obtaining highly-purified HBD-EPO. The structure of recombinant HBD-EPO was close to that of the native EPO protein. HBD-EPO contained two disulfide bonds, as shown by MALDI-TOF mass spectrometry. The protein demonstrated in vitro biological activity… CONTINUE READING
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