Isolation and characterization of a 40-kDa cyclophilin-related protein.

@article{Kieffer1992IsolationAC,
  title={Isolation and characterization of a 40-kDa cyclophilin-related protein.},
  author={Lynda J. Kieffer and Theresia Thalhammer and Robert E. Handschumacher},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 8},
  pages={5503-7}
}
Major and minor isoforms of cyclophilin (CyP-18), a 17.8-kDa protein with peptidyl-prolyl cis-trans isomerase activity, comprise the primary intracellular binding proteins for cyclosporin A. Additional CyP-like proteins with approximate molecular masses of 22 (CyP-22) and 40 kDa (CyP-40) have been recovered from the soluble fraction of calf brain along with CyP-18 by adsorption onto a cyclosporin A affinity column and elution with cyclosporin A. Based on a limited number of peptide sequences… CONTINUE READING
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