Purification and characterization of the chaperonin 10 and chaperonin 60 proteins from Rhodobacter sphaeroides.

@article{Terlesky1991PurificationAC,
  title={Purification and characterization of the chaperonin 10 and chaperonin 60 proteins from Rhodobacter sphaeroides.},
  author={K C Terlesky and F Robert Tabita},
  journal={Biochemistry},
  year={1991},
  volume={30 33},
  pages={8181-6}
}
Two heat-shock proteins that show high identity with the Escherichia coli chaperonin 60 (groEL) and chaperonin 10 (groES) chaperonin proteins were purified and characterized from photolithoautotrophically grown Rhodobacter sphaeroides. The proteins were purified by using sucrose density gradient centrifugation and Mono-Q anion-exchange chromatography. In the presence of 1 mM ATP, the chaperonin 10 and chaperonin 60 proteins bound to each other and comigrated as a large complex during sucrose… CONTINUE READING