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RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms

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Restle,  Tobias
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Restle, T., Müller, B., & Goody, R. S. (1992). RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms. FEBS Letters, 300(1), 97-100. doi:10.1016/0014-5793(92)80172-D.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-AB92-0
Abstract
A method for the rapid preparation of a defined substrate to monitor RNase H activity has been developed. Using this substrate, we have investigated the RNase H activities of the different forms of recombinant HIV-1 and HIV-2 reverse transcriptase (RT) in detail. As we report here, RNase H activity is associated only with the dimeric forms (p51/p66 or p66/p66) of the enzymes.