Abstract
The interaction of rat liver ribosomal proteins L6, L8, L19, S9, and S13 with 5.8 rRNA was characterized by nitrocellulose membrane filtration. Binding approached saturation with the five proteins; the apparent association constants (K'a), measured at 4 degrees C and 22 degrees C, ranged from 0.2 to 18 X 10(5) M-1. The molar ratio of ribosomal protein and rRNA in the complexes at saturation approximated 1, indicating there is one binding site for each of the five proteins on the nucleic acid. A number of ribosomal proteins, including some previously suspected from affinity chromatography of associating weakly, did not form a complex with 5.8 S rRNA.
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.
