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Isolation and Characterization of Natural and Recombinant Cyclophilins

  • T. F. Holzman
  • S. W. Fesik
  • C. Park
  • J. L. Kofron
Part of the Industry-University Cooperative Chemistry Program Symposia book series (IUCC)

Abstract

Cyclophilins (Cyp’s) are members of a class of proteins which bind the pharmaceutically important immunosuppressive agent cyclosporin A (CsA) and its analogs (1–5). In addition to selectively binding CsA, these proteins have proven to be enzymes which accelerate the cis-trans isomerization of proline containing peptide bonds in vitro (8, 9) and the rate of protein folding in vitro (8–13). Recently. another member of the peptidyl-prolyl isomerase family (PPIases) has been identified, the FK binding proteins (FKBP’s) (52, 53). The FKBP’s have very little sequence homology with the Cyp’s and were initially identified as the binding proteins for the potent immunosuppressant FK-506 and its analogs (52–54). Although Cyp and FKBP are both PPIases, they apparently do not have the same specificity for peptide substrates (16) and Cyp will not bind FK-506 nor will FKBP bind CsA (52, 53).

Keywords

Activation Enthalpy Couple Enzymatic Assay Column Flow Rate Bovine Thymus Chymotrypsin Cleavage 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  • T. F. Holzman
    • 1
  • S. W. Fesik
    • 1
  • C. Park
    • 1
  • J. L. Kofron
    • 2
  1. 1.Drug Design and Delivery, Discovery Research, Pharmaceutical Products DivisionAbbott LaboratoriesAbbott ParkUSA
  2. 2.School of PharmacyUniversity of Wisconsin-MadisonUSA

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