Studies on polypeptide-chain-elongation factors from an extreme thermophile, Thermus thermophilus HB8. 3. Molecular properties.

@article{Nakamura1978StudiesOP,
  title={Studies on polypeptide-chain-elongation factors from an extreme thermophile, Thermus thermophilus HB8. 3. Molecular properties.},
  author={Satoko Nakamura and Shunsaku Ohta and Ken‐ichi Arai and Nobutaka Arai and Tairo Oshima and Yoshito Kaziro},
  journal={European journal of biochemistry},
  year={1978},
  volume={92 2},
  pages={533-43}
}
Molecular properties of the polypeptide chain elongation factors from Thermus thermophilus HB8 have been investigated and compared with those from Escherichia coli. 1. As expected, the factors purified from T. thermophilus were exceedingly heat-stable. Even free EF-Tu not complexed with GDP was stable after heating for 5 min at 60 degrees C. 2. GDP binding activity of T. thermophilus EF-Tu was also stable in various protein denaturants, such as 5.5 M urea, 1.5 M guanidine-HCl, and 4 M LiCl. 3… CONTINUE READING