Selective binding of rat liver nuclear enzymes to histones, phosvitin and casein coupled to sepharose.

Abstract

Abstract Phosphoprotein (phosvitin and casein) substituted Sepharoses and histone substituted Sepharoses have been employed for the purification of two cyclic nucleotide independent protein kinases from rat liver nuclei.1, 2 Because of the utility of these columns, two other nuclear enzymes were examined for their ability to btnd to these columns to investigate their possible purification by these techniques. The present communication develops the rationale for the purification of the two nuclear protein kinases (NI and NII) and suggests that these columns will also be useful for the purification of other nuclear enzymes (RNA polymerases and poly (ADP-ri bose)synthetase).