Human Procathepsin D: Three-Dimensional Model and Isolation

  • Gerald Koelsch
  • Peter Metcalf
  • Vaclav Vetvicka
  • Martin Fusek
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 362)


Human procathepsin D was isolated from medium of human breast cancer cell line ZR-75-1 potentiated with estrogen. The isolation involved both immunoaffinity chromatography and ion-exchange chromatography. The affinity chromatography employed polyclonal antibodies raised against a synthetic activation peptide of human cathepsin D. We have started preliminary crystallization trials using the isolated material. A model of human procathepsin D was also built using coordinates of human cathepsin D and pig pepsinogen. The model aids understanding of multiple roles played by activation peptides of aspartic proteinases and will be used as a starting model for molecular replacement.


Human Breast Cancer Cell Line Activation Peptide Aspartic Proteinase Immunoaffinity Chromatography Pair Motif 
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 1995

Authors and Affiliations

  • Gerald Koelsch
    • 1
  • Peter Metcalf
    • 2
  • Vaclav Vetvicka
    • 3
  • Martin Fusek
    • 1
  1. 1.Oklahoma Medical Research FoundationOklahoma CityUSA
  2. 2.European Molecular Biology OrganizationHeidelberg 1Germany
  3. 3.Department of Microbiology and ImmunologyUniversity of LouisvilleLouisvilleUSA

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