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. Author manuscript; available in PMC: 2019 Feb 9.
Published in final edited form as: Biochemistry. 2016 May 4;55(19):2794–2805. doi: 10.1021/acs.biochem.6b00006

Figure 2.

Figure 2.

Effect of anionic detergent and salt on the interaction of Purβ with Acta2 ssDNA. (A) The binding of full-length Purβ (Purβ FL), its core region (Purβ I-II-III), and its intermolecular subdomain (Purβ III) to 0.5 nM PE32-bF ssDNA was assessed in assay buffer containing varying concentrations of sodium deoxycholate. Solid-phase Purβ-PE32-bF complexes were detected by ELISA using rabbit anti-mouse Purβ 210–229 as the primary antibody. (B) The same ELISA format was used to evaluate the effect of varying concentrations of salt on the binding of Purβ FL, Purβ I-II-III, and Purβ III to ssDNA. Data points show absorbance values at 405 nm normalized to the maximum absorbance observed at the lowest concentration of deoxycholate tested (A) or normalized to the absorbance obtained in buffer with 0.15 mM NaCl (B) (mean ± SD, n = 4).