Fig. 3.
Fig. 3. RA-induced conformational changes in wild-type and mutant PML/RARα fusion proteins. / Limited trypsin digestion analysis of wild-type and mutant PML/RARα S-form (A) and L-form (B). In vitro [35S]-methionine synthesized PML/RARα proteins were incubated without (−) or with (+) 1 μmol/L RA, and subsequently treated with increasing trypsin concentrations (0 to 25 μg/mL). Digestion products were analyzed by denaturing electrophoresis. The arrows indicate the intact PML/RARα proteins. Asterisks indicate resistant fragments.

RA-induced conformational changes in wild-type and mutant PML/RARα fusion proteins.

Limited trypsin digestion analysis of wild-type and mutant PML/RARα S-form (A) and L-form (B). In vitro [35S]-methionine synthesized PML/RARα proteins were incubated without (−) or with (+) 1 μmol/L RA, and subsequently treated with increasing trypsin concentrations (0 to 25 μg/mL). Digestion products were analyzed by denaturing electrophoresis. The arrows indicate the intact PML/RARα proteins. Asterisks indicate resistant fragments.

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