Human procathepsin D: three-dimensional model and isolation.

Abstract

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.

• Authors: G Koelsch, P Metcalf, V Vetvicka, M Fusek
• Journal: Advances in experimental medicine and biology (Adv Exp Med Biol) Vol. 362 Pg. 273-8 ( 1995) ISSN: 0065-2598 [Print] United States
• PMID: 8540327 (Publication Type: Comparative Study, Journal Article)

Chemical References

• Enzyme Precursors
• Pepsinogens
• procathepsin D
• Cathepsin D

Topics

• Amino Acid Sequence
• Animals
• Breast Neoplasms
• Cathepsin D (chemistry, isolation & purification)
• Cell Line
• Chromatography, Affinity
• Chromatography, Ion Exchange
• Crystallization
• Crystallography, X-Ray
• Enzyme Precursors (chemistry, isolation & purification)
• Female
• Humans
• Models, Molecular
• Molecular Sequence Data
• Pepsinogens (chemistry)
• Protein Conformation
• Swine
• Tumor Cells, Cultured