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

FEBS Letters

Goody, R.S.¹  Müller, B.¹  Restle, T.¹ 

[1] Abteilung Biophysik, Max-Planck-Institut für medizinische Forschung, Jahnstr. 29, 9600 Heidelberg, Germany

关键词: HIV;    Reverse transcriptase;    RNase H;    Dimerization;    BSA;    bovine serum albumine;    E. coli;    Escherichia coli;    FPLC;    fast protein liquid chromatography;    HIV;    human immunodeficiency virus;    HPLC;    high-performance liquid chromatography;    PCR;    polymerase chain reaction;    RT;    reverse transcriptase;   

DOI  :  10.1016/0014-5793(92)80172-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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

【 授权许可】

Unknown