Fig 3.tif (693.48 kB)
Kinetic characterization of OsttaDSP.
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posted on 2018-01-23, 18:33 authored by Julieta B. Carrillo, Diego F. Gomez-Casati, Mariana Martín, Maria V. BusiA) Effect of pH on the activity of recombinant OsttaDSP. Activity was assayed with pNPP (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) pNPP saturation plot for OsttaDSP determined at pH 7. C) Amylopectin saturation plot for OsttaDSP determined at pH 7.5.
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starch metabolism exhibitsglycogen degradationelectrophoretic homogeneityOstreococcus tauri Ostreococcus tauriArabidopsis thaliana LSF 2.enzyme formsPrasinophyceae familyresidue C 162dephosphorylates amylopectinglucan phosphatasesphosphoglucan phosphatasetauri microalgaeOsttaDSPGlucan phosphatasesgene coding54.5 kDastarch granuleheterologous expression
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