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POL-binding cells

Out of 440000 cells, 17 were capped" rhodamine-stained-POL-binding cells (Table 1). The fluorescein labeling coincided with the rhodamine labeling in 14 cells out of 17. In these cases, no fluorescence was detectable outside the cap. In the rest (3 out of 17) the fluorescein staining was most intense at the rhodamine cap but also could be seen on the rest of the cell surface. Further experiments showed that non-capped immunoglobulin on such cells had anti-POL specificity. This was determined by a double treatment with POL, first... [Pg.24]

POL a 26 ng/ml R-anti- POL Rd R-anti-c MIg FI Additional treatment or pretreatment Capped rhodamine staining (POL-binding cells) Fluorescein labeling coinciding with capped rhodamine staining... [Pg.26]

Pol II associates with other proteins to form a holoenzyme complex. In yeast, at least nine gene products—called Srb (for suppressor of RNA polymerase B)—bind to the CTD. The Srb proteins—or mediators, as they are also called—are essential for pol II transcription, though their exact role in this process has not been defined. Related proteins comprising even more complex forms of RNA polymerase II have been described in human cells. [Pg.351]

Cell debris may be removed by centrifugation at 10,000 g for 30 min. The nucleic acids being the major contaminant can be removed by precipitation with a positively-charged pol)uner such as polyethyleneimine PEI (t)q)ically 0.5-1% of a 10% solution). Addition of magnesium to the resuspension buffer will assist in the enzyme digestion of DNA by DNAse. Some loss of protein may occur by copreciptation, which is especially the case with some DNA-binding proteins. This can usually be avoided by a 1 1 dilution of the crude extract with buffer. [Pg.18]

Amprenavir is a nonpeptide protease inhibitor that is active against both HIV-1 and HIV-2 fosamprenavir is the prodrug for amprenavir and has better bioavailability. After binding to the active site of the viral protease, it inhibits the processing of viral gag and gag-pol polyprotein precursors, resulting in the production of immature HIV particles that lack the capability to infect other cells. The resistance to the drug results from site-directed mutagenesis primarily at codons 50 and 84, and also at codons 10, 32, 46, 54 and 90. [Pg.191]

Eukaryotic cells contain multiple copies of the 5S rRNA gene. Unlike other eukaryotic rRNA genes, the 5S rRNA genes are transcribed by RNA Pol III. Two control elements, an A box and a C box, lie downstream of the transcriptional start site. The C box binds TFIIIA which then recruits TFIIIC. TFIIIB now binds and interacts with RNA Pol III to form the transcription initiation complex. Transcription produces a mature 5S rRNA that requires no processing. [Pg.203]


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See also in sourсe #XX -- [ Pg.25 ]




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