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Nucleic Acids Research, 1980, Vol. 8, No. 5 1167-1185
© 1980

Articles

Hydrophobic affinity chromatography of nucleic acids and proteins

Peter Cashion, Ganesh Sathe, Ali Javed and Joan Kuster

Biology Department, University of New Brunswick Fredericton, New Brunswick, Canada E3B 5A3

Received November 9, 1979. 5' tritylated oligonucleotides binding hydrophobically to low trityl cellulose/sepharose (<15µMTr/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 dependance of these non-covalently anchored ligands permits the isolation of a variety of RNAs including fibroin mRNA. Medium trityl sepharose (15–40µM 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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