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  • Book
    Hollaender, Alexander; Setlow, Jane K.
    Digital Access
    Provider
    Version
    Springer
    v. 27, 2006
    Springer
    v. 28, 2007
    Print Access Request
    Location
    Version
    Call Number
    Items
    Books: General Collection (Downstairs)
    v. 1-28, 1979-2007.
    QH442 .G44
    28
  • Article
    Glick JM, Leboy PS.
    J Biol Chem. 1977 Jul 25;252(14):4790-5.
    An S-adenosylmethionine-dependent tRNA(adenine-1)-methyltransferase has been purified 8,000-fold from rat liver. This preparation gives a single band on polyacrylamide gel electrophoresis and is stable in long term storage. The enzyme has a molecular weight of approximately 95,000. The single methylating capacity of this adenine-1 methyltransferase, using Escherichia coli tRNA2Glu, is methylation of the invariant adenine in the GTpsiC loop. The methylation reaction is dependent on added cation with 20 to 40 mM putrescine being most effective. The Km for S-adenosylmethionine was found to be 0.3 micron, while the Ki for the product inhibitor S-adenosylhomocysteine was 0.85 micron. The Km for tRNAMetf is 12 nM while that for tRNAGlu2 is 33 nM.
    Digital Access Access Options