Related Experiment Video
Updated: Aug 20, 2026

Rapid Production of Recombinant Human SLFN14 Ribonuclease and Stoichiometric Analysis by Mass Photometry
Published on: February 20, 2026
Immunological studies on the interaction of polyadenylic acid and human liver ribonuclease
E A Neuwelt1, W A Gahl, C C Levy
1Baltimore Cancer Research Center, NCI Laboratory of Molecular Biology, 3100 Wyman Park Drive, Baltimore, Maryland 21211, USA.
Abstract:
The effect of polyadenylic acid, a potent inhibitor of mammalian and bacterial RNAses, on the binding of human liver RNAse to its antibody was studied. To do this, a human liver RNAse antibody was immobilized on Sepharose 4B. Examination of the ability of the enzyme to bind to the immobilized anti-RNAse in the presence or absence of polyadenylic acid indicated that enzyme-antibody binding was more sensitive to the presence of polyadenylic acid than was enzyme activity. Furthermore, the effect of polyadenylic acid on enzyme-antibody binding was specific since neither polycytidylic acid nor polyuridylic acid had much effect on the antigenicity of the enzyme. The metal cation, Mg2+, and the polyamine, spermidine, but not putrescine, readily reversed the effects of polyadenylic acid on enzyme-antibody binding.
