10.1371/journal.pone.0191621.g003
Julieta B. Carrillo
Julieta B.
Carrillo
Diego F. Gomez-Casati
Diego
F. Gomez-Casati
Mariana Martín
Mariana
Martín
Maria V. Busi
Maria
V. Busi
Kinetic characterization of OsttaDSP.
Public Library of Science
2018
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 18:33:23
Figure
https://plos.figshare.com/articles/figure/Kinetic_characterization_of_OsttaDSP_/5815056
<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>