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Ribonucleic Acid‐Dependent Ribonucleic Acid Polymerase in the Immune Response
Author(s) -
Saito Kazuko,
Mitsuhashi Susumu
Publication year - 1975
Publication title -
japanese journal of microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0021-5139
DOI - 10.1111/j.1348-0421.1975.tb00959.x
Subject(s) - microbiology and biotechnology , rna , biochemistry , centrifugation , polymerase , rnase p , enzyme , ribosomal rna , rna polymerase , chemistry , enzyme assay , dna , chromatography , biology , gene
Ribonucleic acid (RNA)‐dependent RNA polymerase activity was demonstrated in the microsomal and ribosomal fraction from the spleen cells of immunized mice. The enzyme activity was solubilized by Triton X‐100 from the fraction and partially purified by Biogel A 1.5 M column chromatography. The RNA‐dependent RNA polymerase activity was eluted in a single peak from the column. High activity was demonstrated with an RNA preparation ( i RNA) as template made from the spleens of immunized mice but very low activity was found with an n RNA preparation made from the spleens of normal mice. Incorporation of 3 H‐UTP markedly decreased in the presence of RNase but not in the presence of DNase. DNA preparations made from the spleens of immunized mice were inactive as template for this enzyme. The i RNA preparation was fractionated by sucrose density gradient centrifugation. A fraction corresponding to 12–13 S was most active as a template. It was followed by a fraction corresponding to 6–7 S. Sucrose gradient analysis of the 3 H‐UTP‐labeled product was attempted. Some properties of this enzyme are described.