Immunological studies on the interaction of polyadenylic acid and human liver ribonuclease

Edward A. Neuwelt, William A. Gahl, Carl C. Levy

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)885-893
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume73
Issue number4
DOIs
StatePublished - Dec 20 1976

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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