Hydrophobic affinity chromatography of nucleic acids and proteins

Hydrophobic affinity chromatography of nucleic acids and proteins.

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 thes...

Hydrophobic Affinity Chromatography of Proteins

1. Chromatographic studies have been made of the affinities of a number of purified proteins for agarose (Sepharose 4B) substituted with 4-phenylbutylamine (PBA) or with E-aminocaproyl-n-tryptophan methyl ester (ACTME) as compared to controls of untreated agarose and/or of cyanogen bromide treated agarose without addition of a substituting amine. 2. At pH 8, cu-chymotrypsin (3.4.4.5) and 7s y-g...

Nucleic acids and proteins

Nucleic Acids and Proteins

Detergent-enabled transport of proteins and nucleic acids through hydrophobic solvents.

It is demonstrated that proteins and nucleic acids can be transported through hydrophobic organic solvents (liquid membranes) via nonspecific complex formation with detergents, whereas no macromolecule transport is observed without the latter. A protein (or a nucleic acid) first interacts with an oppositely charged detergent due to hydrophobic ion pairing in the aqueous feed phase. The resultan...