Potential Importance of Metal-Ligand Interactions in Enzyme Assays Demonstrated with the Assay Cocktail for Phosphoenolpyruvate Carboxylase | Zendy

William H. Outlaw | Zendy

Open Access

Potential Importance of Metal-Ligand Interactions in Enzyme Assays Demonstrated with the Assay Cocktail for Phosphoenolpyruvate Carboxylase

Author(s) -

William H. Outlaw

Publication year - 1990

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.92.2.528

Subject(s) - pyruvate carboxylase , phosphoenolpyruvate carboxylase , substrate (aquarium) , enzyme , effector , chemistry , ligand (biochemistry) , biochemistry , limiting , phosphoenolpyruvate carboxykinase , enol , biology , catalysis , receptor , mechanical engineering , ecology , engineering

Assay cocktail modification such as addition of effector can cause inadvertent changes in the concentration of other metalligand and free species. In some cases, e.g. in the assay for phosphoenolpyruvate carboxylase under a limiting-substrate condition, unintentional changes in substrate concentration are significant and confound an interpretation based solely on the total concentration of each component. A cautionary argument is developed on the basis of examples from the current literature.

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