Purification and characterization of chaperonin 10 from Chromatium vinosum.

@article{TorresRuiz1992PurificationAC,
  title={Purification and characterization of chaperonin 10 from Chromatium vinosum.},
  author={Jos{\'e} A. Torres-Ruiz and B A Mcfadden},
  journal={Archives of biochemistry and biophysics},
  year={1992},
  volume={295 1},
  pages={172-9}
}
Chromatium vinosum contains a polypeptide that is functionally and structurally similar to the Escherichia coli chaperonin 10. The protein has been purified to homogeneity by sucrose density gradient centrifugation followed by gel filtration using a Bio-Gel A-1.5 m column. The molecular mass of chaperonin 10, as determined by gel filtration or nondenaturing polyacrylamide gel electrophoresis, is 95 kDa. The oligomer is composed of seven or eight subunits. Comparisons of the overall amino acid… CONTINUE READING