D-Lactate Dehydrogenase (D-LDH), Grade II from Lactobacillus delbrückii, lyophilizate Dehydrogenase that catalyzes the interconversion of D(-)-lactate to pyruvate. Application Use D-Lactate Dehydrogenase (D-LDH), Grade II, in a variety of diagnos- tic tests, e.g., in the determination of alanine aminotransferases, lactate or pyruvate. Used for the removal of pyruvate in determinations working with NADH (i.e., triglycerides, lipase, aldolase, aspartate aminotransferases, gluta- mat dehydrogenase). Benefits Rely on the proven diagnostic quality of this product. EC 1.1.1.28 Properties Nomenclature: D-lactate:NAD + oxidoreductase Michaelis constants (Tris maleate buffer, pH 8.0, +25°C): D-lactate: 0.7 x 10 -1 mol/l (NAD, 2 mmol/l) Pyruvate: 1.2 x 10 -3 mol/l (NADH, 0.1 mmol/l) NADH: 7.1 x 10 -5 mol/l (pyruvate, 20 mmol/l) pH optimum: 7.0 (see figure) Temperature dependence: See figure pH stability: 4.0-10.0 (see figure) Thermal stability: Up to +50°C (see figure) Specificity: Lactate dehydrogenase is specific for D(–)-lactate, L(+)-lactate does not react.