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Updated: Oct 2, 2026
Preparation of Chloroplast Sub-compartments from Arabidopsis for the Analysis of Protein Localization by Immunoblotting or Proteomics
Published on: October 19, 2018
Overproduction, purification, and characterization of recombinant aspartate semialdehyde dehydrogenase from
Stephane Paris1, Peter M Wessel, Renaud Dumas
1Unité Mixte CNRS/INRA/Aventis CropScience, UMR 1932, 14-20 Rue Pierre Baizet, 69263 Lyon, France.
Abstract:
In plant and microorganisms, aspartate semialdehyde dehydrogenase (ASDH) produces the branch point intermediate between the lysine and threonine/methionine pathways. In this study, we report the first cDNA cloning, purification, and characterization of a plant ASDH. The Arabidopsis thaliana ASDH is an homodimeric enzyme composed of subunits of 36 kDa. The plant enzyme exhibited a specific activity of 26 micromol NADPH oxidized min(-1) mg(-1) of protein with a K(M) value for NADPH of 92 microM. ASDH showed cooperative behavior for aspartyl phosphate with a K(0.5) value of 37 microM.
