Chemical modification of the phosphoenolpyruvate carboxylase from maize leaves and its conformation in isotropic solution. Studies via triplet lifetime and rotational diffusion using eosin isothiocyanate as label
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
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1. Kinetics and equilibrium binding of phosphoenolpyruvate to phosphoenolpyruvate carboxylase from Zea mays;Physical Chemistry Chemical Physics;1999
2. Site-directed mutagenesis ofFlaveria trinerviaphosphoenolpyruvate carboxylase: Arg450and Arg767are essential for catalytic activity and Lys829affects substrate binding;FEBS Letters;1996-09-02
3. Site-directed mutagenesis of Lys600 in phosphoenol pyruvate carboxylase of Flaveria trinervia : its roles in catalytic and regulatory functions;FEBS Letters;1995-11-13
4. Purification and Characterization of Phosphoenolpyruvate Carboxylase from Developing Seeds of Brassica;Journal of Plant Biochemistry and Biotechnology;1995-01
5. Modification of Maize Leaf Phosphoenolpyruvate Carboxylase with Fluorescein Isothiocyanate1;Plant and Cell Physiology;1994
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