Purification and characterization of RNase-inhibitor complex from rat reticulocytes.

During purification of the RNase-inhibitor complex from rat reticulocytes, two forms of the complex were separated by DEAE-Sephadex chromatography. One complex was purified 10,000-fold from the cell lysate, and the other 1,000-fold. Both complexes were shown to be composed of 1 mol of RNase and 1 mol of inhibitor. Reconstitution experiments revealed that the multiplicity of the complex was primarily due to differences in the RNase. The RNases derived from the two complexes differed in their sensitivities to metal ions and hemin.