Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
