Description_x000D_ General description_x000D_ Glycerol 3-phosphate Oxidase is a FAD-dependent α-glycerophosphate oxidase and catalyzes the formation of dihydroxyacetonephosphate. Glycerol 3-phosphate oxidase comprises of a flavin adenine dinucleotide (FAD) and a substrate binding domain and corresponds to molecular weight of 42 kDa. It exists as a monomer and the active site comprises of isoalloxazine ring and histidine 53, arginine 316 and lysine 345 residues crucial for ligand binding._x000D_ Application_x000D_ Glycerol 3-phosphate Oxidase from Pediococcus sp. has been used in the kinetic assay to study gluconeogenesis in liver and in immobilization studies on pencil graphite (PG) electrode._x000D_ Packaging_x000D_ 100 units in glass bottle_x000D_ Physical properties_x000D_ Isoelectric point : 4.1 -/+0.1_x000D_ Michaelis constants : 3.2x10 -3M (L-α-Glycerophosphate), 6.8 x 10 -3M (D, L-form)_x000D_ Inhibitors : Ionic detergents (SDS, LBS, etc.), Hg++, Ag+_x000D_ Optimum pH : 8.0 - 8.5Optimum temperature : 35 - 40oC_x000D_ pH Stability : pH 6.5 - 8.5 (25oC, 20hr) Thermal stability : below 40oC (pH 7.0, 15min)_x000D_ Substrate specificity : The enzyme has the highest specificity for L-form of a-γlycerophosphate_x000D_ Unit Definition_x000D_ One unit will oxidize 1.0 μmole of L-glycerol 3-phosphate to dihydroxyacetone phosphate with the formation of H2O2 per min at 37°C, at the appropriate pH._x000D_ Physical form_x000D_ Lyophilized powder containing stabilizers