Hydrophobic affinity chromatography of nucleic acids and proteins. II. Activity of trityl Sepharose immobilized enzymes.
A variety of nucleic acid synthetic and degradative enzymes and proteases are shown to bind to trityl sepharose columns and, for the most part, retain moderate amounts of activity for periods of days to weeks. Non-covalent hydrophobic interactions are believed to be largely responsible for the observed binding and maintenance of activity. In addition the hydrophobic binding mechanism of poly A to trityl sepharose columns under a variety of conditions is compared with that to nitrocellulose columns and contrasted with that of dT cellulose columns.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000378:metabolism; D002846:Chromatography, Affinity / Q000379:methods; D004247:DNA / Q000302:isolation & purification; D003851:Deoxyribonucleases / Q000378:metabolism; D004355:Drug Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D008836:Micrococcal Nuclease / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D011061:Poly A / Q000302:isolation & purification*; D011117:Polyribonucleotide Nucleotidyltransferase / Q000378:metabolism; D011131:Polyribonucleotides / Q000302:isolation & purification*; D011506:Proteins / Q000302:isolation & purification; D012313:RNA / Q000302:isolation & purification; D012685:Sepharose / Q000031:analogs & derivatives
D004800:Enzymes, Immobilized; D011131:Polyribonucleotides; D011506:Proteins; C031045:trityl-agarose; D011061:Poly A; D012313:RNA; D004247:DNA; D012685:Sepharose; D011117:Polyribonucleotide Nucleotidyltransferase; D003851:Deoxyribonucleases; D000469:Alkaline Phosphatase; D010744:Phosphoric Monoester Hydrolases; D008836:Micrococcal Nuclease; D010447:Peptide Hydrolases; D000251:Adenosine Triphosphatases