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Variation in Apparent Enzyme Activity in Two‐Enzyme Assay Systems: Phosphoenolpyruvate Carboxylase And Malate Dehydrogenase
Author(s) -
Hatley RH,
Franks F.
Publication year - 1989
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1989.tb00066.x
Subject(s) - phosphoenolpyruvate carboxylase , malate dehydrogenase , phosphoenolpyruvate carboxykinase , enzyme , biochemistry , pyruvate carboxylase , glycerol , enzyme assay , biology , citrate synthase , lactate dehydrogenase , chemistry
We have employed the two‐enzyme assay system for phosphoenolpyruvate to investigate the effect on the apparent phosphoenolpyruvate carboxylase (PEP‐C) activity of the use of malate dehyrogenase (MDH) that has been stabilized in either glycerol or (NH4)2SO4. The type of MDH stabilizer has a marked effect on the apparent activity of the PEP‐C. The apparent activities of the PEP‐C are 1.34 and 0.43 U/mg in the presence of glycerol and salt‐stabilized MDH, respectively. The implications of the observations for diagnostic assays are discussed.