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Reverse transcriptase from simian foamy virus serotype 1: purification and characterization.

A B Benzair, A Rhodes-Feuillette, R Emanoïl-Ravicovitch

    Journal of Virology
    |November 1, 1982
    PubMed
    Summary

    Researchers purified simian foamy virus type 1 reverse transcriptase using heparin-Sepharose chromatography. The enzyme, with a molecular weight of 81,000, requires a ribonucleotide template or DNA primer for activity.

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    Virology·1997

    Area of Science:

    • Virology
    • Molecular Biology
    • Biochemistry

    Background:

    • Simian foamy virus type 1 (SFV-1) is a primate retrovirus.
    • Viral RNA-dependent DNA polymerase (reverse transcriptase) is crucial for retroviral replication.
    • Purification of SFV-1 reverse transcriptase is necessary to study its enzymatic properties.

    Purpose of the Study:

    • To purify the reverse transcriptase from SFV-1 core polypeptides.
    • To characterize the purified enzyme's molecular weight and activity requirements.
    • To investigate the enzyme's kinetic properties and structural features.

    Main Methods:

    • Heparin-Sepharose chromatography was employed for enzyme purification.
    • Specific activity and molecular weight were determined.

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  • Enzyme activity assays were performed using various template-primer combinations.
  • Heat inactivation studies were conducted.

    • Main Results:

    • Highly purified SFV-1 reverse transcriptase was obtained with high specific activity.
    • The enzyme is monomeric with an average molecular weight of 81,000.
    • Activity requires a ribonucleotide template or DNA with 3'-OH ends.
    • Heat inactivation suggests two distinct functional loci on the enzyme.

    Conclusions:

    • Heparin-Sepharose is an effective method for purifying SFV-1 reverse transcriptase.
    • The enzyme's characteristics are comparable to other primate retroviral reverse transcriptases.
    • The enzyme exhibits distinct substrate and template-primer binding sites.