A comparison of the chromatographic properties of various polyadenylate binding materials

Mercer, J. F. B.; Naora, Honami

doi:10.1016/s0021-9673(00)85248-6

Cited by 10 publications

(4 citation statements)

References 29 publications

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“…DMTr(Cp)6(4)+poly G (5) 40% poly G bound2'3 6. DMTr(Cp)15(10)+poly G (9) 50% poly G bound ' ' 7. DMTr(ACCAGC)2(8)+FmRNA(5000CPM) 80% binding5…”

Section: Experiments Resultsmentioning

confidence: 99%

“…TRs are very stable, some being used for 7 years without any apparent capacity loss; dT cellulose and poly U sepharose (to a lesser degree) are also stable, but with extended use nuclease damage and attendent capacity loss might be incurred. The benzoyl ester linkage in benzoyl cellulose or derivatives is reported to be somewhat unstable (8,9). A (8) and the closer packing of its fibers, more "irreversible" binding was seen with TC than with TS columns.…”

Section: Methodsmentioning

confidence: 99%

“…This report details: 1) the specificity and mechanism of polynucleotide binding to TRs; 2) the use of S'tritylated oligomers as affinity ligands, operating by means of H-bonds; 3) the binding of proteins to TRs. Upon reviewing the literature with regard to poly A (8,9), DNA (10) or viral RNA (11) binding to cellulose or to aromatic cellulose derivatives many precedents were found. The specificity of these columns, was rather weak in tha-t both poly U and poly A were bound.…”

Section: Introductionmentioning

confidence: 99%

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Hydrophobic affinity chromatography of nucleic acids and proteins

et al. 1980

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5' tritylated oligonucleotides binding hydrophobically to low trityl cellulose/sepharose (< 15 microMTr/ml) retain their hydrogen-bonding specificities for complementary sequences. This, constitutes a novel mode of attaching affinity ligands to solid supports, is more convenient than existing methods, and proceeds with 100% yield. The salt, dielectric constant and temperature dependence of these non-covalently anchored ligands permits the isolation of a variety of RNAs including fibroin mRNA. Medium trityl sepharose (15-40 microM Tr/ml) has a high binding specificity for poly A and poly A containing mRNA, equivalent to dT cellulose. Most proteins, including nucleic acid enzymes, bind to these columns and retain enzymatic activity, thus mimicking enzymes attached covalently to solid phases. A number of in vivo counterparts to this hydrophobically determined specificity are noted, as are homologies to nitro-cellulose filters.

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“…DMTr(Cp)6(4)+poly G (5) 40% poly G bound2'3 6. DMTr(Cp)15(10)+poly G (9) 50% poly G bound ' ' 7. DMTr(ACCAGC)2(8)+FmRNA(5000CPM) 80% binding5…”

Section: Experiments Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Hydrophobic affinity chromatography of nucleic acids and proteins

et al. 1980

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“…The binding capacity of oligo(dT)-matrices 5 increases with salt concentration up to about 500 mM NaCl, KCl, or LiCl, though the binding capacity is greater when KCl or LiCl is used in place of an equivalent amount of NaCl (Mercer and Naora, 1975). This increase in binding capacity, however, may be accompanied by an increase in non-specific hybridization to the matrix.…”

Section: Selection Of Polyadenylated Moleculesmentioning

confidence: 99%