Fructose–1,6–bisphosphate aldolase (E.C. 4.1.2.13) is a major glycolytic enzyme found in most cells. Fructose-1,6- bisphosphate aldolase reversibly catalyses the cleavage of fructose 1,6-bisphosphate into the triose phosphates: Dglyceraldehyde phosphate and dihydroxyacetone phosphate. In this study, we wanted to examine the presence of aldolase in healthy human placenta and then to purify the enzyme. We also determined the optimum conditions (time, pH, and temperature) of enzyme assay measurements. With this procedure, we determined the specific activity of placental aldolase as 831.90 mU/mg protein and aldolase was purified about 40.5 fold from healthy human placenta. It was demonstrated that the molecular weight of human placental aldolase was 160 kD. In this study, substrate kinetics were also examined. Enzymatic assays were performed and substrate kinetic properties were detected and Vm value of healthy placental FBPA was determined as 1769.513 ± 200.322, and Km as 20.003 ± 4.497 mM.

Keywords: