Fig. 3.
Fig. 3. Western blot of PARP proteolysis on treatment of Molt-4 cells with GW1843. Molt-4 cells in log-phase growth were treated with 8 nmol/L GW1843 and aliquots of 2 × 106 cells were taken at the indicated times. Cells were prepared for electrophoresis, electrophoresed on 7.5% polyacrylamide SDS gels,29 and blotted onto nitrocellulose as described in Materials and Methods. The blot is an x-ray film image of PARP protein detected with a horseradish peroxidase-conjugated secondary antibody visualized with chemiluminescent substrate (Amersham) blotted as described in Materials and Methods. The Mr values were determined by running prestained Mr markers (BioRad). Intact PARP (upper band) is Mr 116,000 and the proteolytic fragment is Mr 85,000. This blot is from a representative experiment from four separate determinations.

Western blot of PARP proteolysis on treatment of Molt-4 cells with GW1843. Molt-4 cells in log-phase growth were treated with 8 nmol/L GW1843 and aliquots of 2 × 106 cells were taken at the indicated times. Cells were prepared for electrophoresis, electrophoresed on 7.5% polyacrylamide SDS gels,29 and blotted onto nitrocellulose as described in Materials and Methods. The blot is an x-ray film image of PARP protein detected with a horseradish peroxidase-conjugated secondary antibody visualized with chemiluminescent substrate (Amersham) blotted as described in Materials and Methods. The Mr values were determined by running prestained Mr markers (BioRad). Intact PARP (upper band) is Mr 116,000 and the proteolytic fragment is Mr 85,000. This blot is from a representative experiment from four separate determinations.

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