Adsorption of Ammonia by Proteins by Bancroft W. D. PDF

By Bancroft W. D.

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Influence of the gel concentration, voltage, and running temperature on the formation of protein–DNA complexes in EMSA. A synthetic double-stranded oligonucleotide bearing the high-affinity binding site for the transcription factor Sp1 was 5¢-end labeled and incubated with (C+) or without (C−) 5 µg crude nuclear extract from human epithelioid carcinoma HeLa (ATCC CCL 2) cells. The EMSAs were run at 4°C on native polyacrylamide gels whose concentration ranged from 4 to 12% (a), on a 6% gel runned at two different temperatures (4°C and room temperature (RT)) (b) or at three different voltages (60, 120, and 200 V) on either 6 and 10% polyacrylamide gels (c).

1997). Transcriptional regulation of the rat poly(ADPribose) polymerase gene by Sp1. Eur. J. Biochem. 250, 342–353. , de Murcia, G. and Schnarr, M. (1988). Specific protein– DNA complexes: immunodetection of the protein component after gel electrophoresis and Western blotting. Anal. Biochem. 174, 235–238. K. C. (1999). Electrophoretic mobility shift assay coupled with immunoblotting for the identification of DNA-binding proteins. Biotechniques 27, 887–890, 892. , Harbers, M. and Vennström, B. (1993).

Biotechniques 18, 704–706. W. F. (1998). Use of modified agarose gel electrophoresis to resolve protein–DNA complexes for electrophoretic mobility shift assay. Biotechniques 24, 216–218. 33 17. Revzin, A. (1989). Gel electrophoresis assays for DNA–protein interactions. Biotechniques 7, 346–355. 18. , Dai, W. L. (1993). Enhanced gel mobility shift assay for DNA-binding factors. Anal. Biochem. 213, 162–167. 19. C. and Ehrlich, M. (1992). Increasing the activity of affinity-purified DNA-binding proteins by adding high concentrations of nonspecific proteins.

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Adsorption of Ammonia by Proteins by Bancroft W. D.


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