Key result
Anti-ribonuclease F1 antibodies completely inhibit enzyme activity on RNA substrates and reveal multiple epitopes.
Antibodies raised against RNase F1 successfully inhibited its enzyme activity and demonstrated weak cross-reactivity with RNases Ms and T1 on Western blot.
Should not yet change clinical practice; extends RNase epitope mapping and supports specific enzyme inhibition in research.
Antibody against ribonuclease (RNase) F1 was raised in a rabbit by intramuscular injection of the protein with Freund’s complete adjuvant. Excess amount of the antibody totally inhibited the enzyme activity on RNA substrate. Quantitative precipitin analysis showed the presence of at least 4 or 5 epitopes (antigenic determinants) on the RNase F1 molecule. Cross-reactivity of the antibody with RNases T1, Ms, U2, St and T2 was examined. Although the double diffusion test detected no cross-reactivity with any of these RNases, Western blot analysis with anti RNase F1 antibody revealed weak cross-reactivity with RNases Ms and T1.
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吉田 et al. (2010) studied this question. Anti-ribonuclease F1 antibodies completely inhibited enzyme activity on RNA substrates and revealed at least 4 or 5 epitopes on the RNase F1 molecule.
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