期刊论文详细信息
FEBS Letters | |
RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms | |
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
【 预 览 】
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