Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.

@article{Nagai1985OxygenBP,
  title={Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.},
  author={Kiyoshi Nagai and Max F. Perutz and Claude Poyart},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1985},
  volume={82 21},
  pages={7252-5}
}
Human beta-globin was synthesized in Escherichia coli as a cleavable fusion protein, using the expression vector pLcIIFX beta-globin [Nagai, K. & Thøgersen, H. C. (1984) Nature (London) 309, 810-812]. The fusion protein cIIFX beta-globin was purified to homogeneity and cleaved at the junction by blood coagulation factor Xa; the authentic beta-globin was liberated. Beta-globin was folded in vitro and reconstituted with heme and alpha subunits to form alpha 2 beta 2 tetramers. The oxygen binding… CONTINUE READING
24 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 24 extracted citations

Similar Papers

Loading similar papers…