ABSTRACT
Template chromatography has been used successfully in the purification of several proteins. Many proteins that operate in association with intracellular DNA recognize purified DNA as a substrate and bind tightly to it at physiological ionic strengths in vitro. The amino acid and carbohydrate analyses revealed that each of these fractions has a protein moiety in coinmon with RNase T2 and the heterogeneities were due to the carbohydrate content, primarily galactose content. The similarities between the proteins from cyanobacteria and E. coli suggest a degree of evolutionary conservation comparable to that of the histones of eukaryotes. DNA-cellulose chromatography has been used to isolate single stranded binding proteins from Tetrahymena thermophila. The proteins that have a high binding affinity to myosin mRNA also have a discriminating effect when added to a wheat germ system containing myosin and globin mRNA. Both myosin mRNA and globin mRNA have been bound to activated Sepharose 4B.
