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Human procathepsin D: three-dimensional model and isolation.

G Koelsch·P Metcalf·V Vetvicka·M Fusek
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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.

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Amino Acid SequenceAnimalsBreast NeoplasmsCathepsin DCell LineChromatography, AffinityChromatography, Ion ExchangeCrystallizationCrystallography, X-RayEnzyme PrecursorsFemaleHumansModels, MolecularMolecular Sequence DataPepsinogensProtein ConformationSwineTumor Cells, CulturedComparative StudyJournal Article

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G Koelsch, P Metcalf, V Vetvicka, M Fusek. 1995. Human procathepsin D: three-dimensional model and isolation.. https://doi.org/10.1007/978-1-4615-1871-6_31

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