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- W2382971882 abstract "Objective:To separate and purify the RFA binding protein and identify the protein, which will facilitate the further study of RFA protein interaction and its function in AR mediated expression of PSA gene. Methods:The human prostate cancer cell line PC 3 was incubated in vitro to extract the nuclear proteins, and from which the RFA binding protein was purified by DNA affinity chromatography using RFA as probe. Before and after chromatography, the function of the RFA binding protein was detected by electrophoretic mobility shift assay (EMSA). After determining the molecular weight of the purified protein by SDS PAGE, the band was excised from gel for protein identification.Results:Amino acid sequencing and mass spectrometric analysis indicated that the band contained two proteins, which possessed sequences closely homologous to heterogeneous nuclear ribonucleoprotein A1, A2 (hnRNP A1, A2). Conclusion:①The method using Dynal M 280 magnetic particles coated with streptavidin for affinity chromatography has many advantages such as convenient, fast and nontoxic, which can purify a protein without knowing it in detail;②The RFA binding proteins are closely homologous to hnRNP A1, A2, which are the components of hnRNP superfamily, so the detail mechanism and the significance of RFA interaction with its binding protein is still waiting further study." @default.
- W2382971882 created "2016-06-24" @default.
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- W2382971882 date "2001-01-01" @default.
- W2382971882 modified "2023-09-25" @default.
- W2382971882 title "SEPARATION AND PURIFICATION OF A NUCLEAR PROTEIN OF PROSTATE CELLS BY DNA AFFINITY CHROMATOGRAPHY" @default.
- W2382971882 hasPublicationYear "2001" @default.
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