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- W302319329 abstract "Publisher Summary This chapter describes the role of affinity chromatography in the purification and characterization of proteins of heterogeneous nuclear ribonucleoprotein complexes. Affinity chromatographic methods for purification of proteins rely on the specificity and relatively high affinity of a protein for an immobilized substrate. Among the advantages of the large scale purification of hnRNP proteins by affinity chromatography on ssDNA are its relative rapidity and ease, its independence of the intactness of hnRNP particles during sample preparation, the lack of a need for radioactive labeling of the hnRNA for detection of the hnRNP-containing fractions, and the stability of the ssDNA column. Addition of a heparin wash (1.0 mg/ml in 100 mM NaC1) after the binding results in greater purity of the fractions, most probably owing to the competition for those proteins that bind to the column predominantly via ionic interactions with the DNA phosphate backbone. Adjustment of the nucleoplasm salt content to lower concentrations results in increased binding of a larger number of hnRNPs to the ribohomopolymers." @default.
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- W302319329 date "1990-01-01" @default.
- W302319329 modified "2023-09-24" @default.
- W302319329 title "Purification and characterization of proteins of heterogeneous nuclear ribonucleoprotein complexes by affinity chromatography" @default.
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- W302319329 doi "https://doi.org/10.1016/0076-6879(90)81133-f" @default.
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