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Reverse transcriptase from avian myeloblastosis virus

G E Houts, M Miyagi, C Ellis

    Journal of Virology
    |February 1, 1979
    PubMed
    Summary
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    Researchers purified avian myeloblastosis virus RNA-dependent DNA polymerase to over 95% purity using a two-step chromatography method. This yielded substantial enzyme quantities with high specific activity, free of RNase.

    Area of Science:

    • Molecular Biology
    • Virology
    • Enzymology

    Background:

    • Avian myeloblastosis virus (AMV) is a retrovirus known to possess RNA-dependent DNA polymerase activity.
    • Efficient purification of this enzyme is crucial for biochemical and genetic studies.

    Purpose of the Study:

    • To develop a robust method for high-purity isolation of AMV RNA-dependent DNA polymerase.
    • To characterize the purified enzyme's properties.

    Main Methods:

    • A two-step column chromatography procedure was employed using DEAE (DE 52) and carboxymethylcellulose (CM 52).
    • Enzyme purity was assessed, and yields were quantified.

    Main Results:

    • Preparations achieved greater than 95% purity for RNA-dependent DNA polymerase.

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  • Yields ranged from 20,000 to 35,000 U/g of virus, with specific activity of 35,000 to 60,000 U/mg protein.
  • The purified enzyme had a molecular weight of ~160,000, an isoelectric point of 6.5, and was free of detectable RNase activity.

    • Conclusions:

    • The described chromatographic method effectively purifies AMV RNA-dependent DNA polymerase to high standards.
    • The characterized enzyme is suitable for further molecular studies.