α-Glycerophosphate Dehydrogenase-Triosephosphate

α-Glycerophosphate Dehydrogenase-Triosephosphate (GDH-TIM) (2 mg/mL) provides sufficient excess enzyme activity to enable accurate measurement of transketolase activity in human erythrocyte hemolysates via NADH oxidation, with no interfering transketolase activity present in the suspension^[1].
α-Glycerophosphate Dehydrogenase-Triosephosphate Isomerase (6.8-90 U/mL) incorporated into the amperometric aldolase assay in a cell-free biochemical system greatly increases assay sensitivity by enabling consumption of 2 moles of NADH per mole of FDP and making the aldolase reaction rate-limiting^[2].
α-Glycerophosphate Dehydrogenase-Triosephosphate (5 units; incubated at 25 °C until absorbance stabilized prior to Rubisco addition) enables spectrophotometric measurement of Rubisco activity in Vinca minor leaf tissue, revealing that transgenic Vinca minor plants have half the Rubisco activity of non-transgenic controls (1.80 milliunits mL^-1 mg protein^-1 vs. 3.61 milliunits mL^-1 mg protein^-1)^[3].
α-Glycerophosphate Dehydrogenase-Triosephosphate (8 units/mL) functions as a coupling enzyme to quantify glyceraldehyde-3-phosphate via NADH absorbance measurement in cell-free biochemical assays for FSA kinetic analysis^[4].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.