Carrillo, Julieta B. F. Gomez-Casati, Diego Martín, Mariana V. Busi, Maria Kinetic characterization of OsttaDSP. <p><b>A) Effect of pH on the activity of recombinant OsttaDSP.</b> Activity was assayed with <i>p</i>NPP (filled triangles/▲) or amylopectin (filled circles/●) as a substrate using 100 mM Sodium Acetate, 50 mMBis-Tris and 50 mM Tris as a buffer. Buffer pH values were adjusted to the values shown in the graphic and used to assay the enzyme. All data are the means ± SD of 3 independent experiments. <b>B) <i>p</i>NPP saturation plot for OsttaDSP determined at pH 7. C) Amylopectin saturation plot for OsttaDSP determined at pH 7.5.</b></p> starch metabolism exhibits;glycogen degradation;electrophoretic homogeneity;Ostreococcus tauri Ostreococcus tauri;Arabidopsis thaliana LSF 2.;enzyme forms;Prasinophyceae family;residue C 162;dephosphorylates amylopectin;glucan phosphatases;phosphoglucan phosphatase;tauri microalgae;OsttaDSP;Glucan phosphatases;gene coding;54.5 kDa;starch granule;heterologous expression 2018-01-23
    https://plos.figshare.com/articles/figure/Kinetic_characterization_of_OsttaDSP_/5815056
10.1371/journal.pone.0191621.g003