Immunological studies on the interaction of polyadenylic acid and human liver ribonuclease.
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.
Neuwelt
E A
EA
Baltimore Cancer Research Center, NCI Laboratory of Molecular Biology, 3100 Wyman Park Drive, Baltimore, Maryland 21211, USA.
Gahl
W A
WA
Levy
C C
CC
D000906:Antibodies / Q000276:immunology*; D000941:Antigens / Q000276:immunology; D001666:Binding Sites, Antibody / Q000276:immunology*; D002847:Chromatography, Agarose; D006801:Humans; D008099:Liver / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D011061:Poly A / Q000494:pharmacology*; D011066:Poly C / Q000494:pharmacology; D011700:Putrescine / Q000494:pharmacology; D012260:Ribonucleases / Q000037:antagonists & inhibitors* / Q000276:immunology*; D012680:Sensitivity and Specificity; D013095:Spermidine / Q000494:pharmacology
D000906:Antibodies; D000941:Antigens; D011061:Poly A; D011066:Poly C; D012260:Ribonucleases; D008274:Magnesium; D013095:Spermidine; D011700:Putrescine