Affinity purification and characterization of (2'-5')oligo(adenylate)-dependent RNase from mouse spleen.

Abstract

Murine (2'-5')An-dependent RNase, a key enzyme of the interferon system, was purified from mouse spleen by affinity chromatography to immobilized (2'-5')An. Since the ribonuclease has high affinity to (2'-5')An, optimal non-denaturing conditions were obtained to disrupt the (2'-5')An-nuclease complex. Low-pH buffers in the presence of 0.1% Triton X-100… (More)

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@article{Bayard1994AffinityPA, title={Affinity purification and characterization of (2'-5')oligo(adenylate)-dependent RNase from mouse spleen.}, author={Bernard Bayard and Pascale Bette-Bobillo and Sigrid Aliau}, journal={European journal of biochemistry}, year={1994}, volume={223 2}, pages={403-10} }