Ribonuclease activity in preparations of human leukocyte interferon
Khesin, I.E.; Aliab'eva, T.N.; Malinovskaia, V.V.; Kuznetsov, V.P.; Gerasimov, A.M.
Biulleten' Eksperimental'noi Biologii i Meditsiny 82(7): 805-807
1976
ISSN/ISBN: 0365-9615 PMID: 8177 Document Number: 100151
Preparations of human leukocyte interferon obtained by multi-stage purification procedure exhibited ribonuclease activity with the optimum at pH 7.0--7.5. The enzyme possessed the endonuclease action mechanism. Most substances studied for their effect on the RNA-ase activity in human interferon preparations showed many of them to act on the enzyme in the same way as on other ribonucleases. However, dithioerythritie, a reducing agent for disulfide bounds, activated the ribonuclease in the interferon preparation, as distinct from the pancreatic ribonuclease, which was inhibited by this preparation. Patterns of protein and RNA-ase distribution were obtained by electrophoresis in polyacrylamide gel.