The Interactions of Korean Panax Ginseng on Glycogen Phosphorylase b and Its Subsequent Effect on Enzyme Kinetics

Voiceover

Presenter(s)

Jake Jardon

Abstract or Description

Glycogen phosphorylase b is an enzyme categorized by its function of catabolism of glycogen into glucose-1-phosphate subunits, thus playing a critical role in the production of cellular energy equivalents. The enzymatic activity of glycogen phosphorylase b can be modulated allosterically by an array of effector molecules which can further be categorized into activators and inhibitors. Korean panax ginseng is a root derived supplement which is marketed on the assertion of an increase in energy. The interaction and subsequent effector activity of Korean panax ginseng on the catabolic enzyme kinetics of glycogen phosphorylase b was the focus of this investigation. To study the interactions and effect of Korean panax ginseng on the enzymatic activity of glycogen phosphorylase b, beer-lambert's law was employed to correlate recorded absorbance values to a reaction solutions inorganic phosphate concentration, which was proportional to the rate of glycogen catabolism. Two comparative assays were completed using known activator AMP and known inhibitor ATP. A third assay using Korean panax ginseng was completed to categorize its effects on glycogen phosphorylase b. In all three assays the Michaelis-Menten kinetics model was used to analyze the effects of increasing effector concentrations on enzyme activity. The data collected showed a positive correlation between the concentration of Korean panax ginseng and the maximum velocity of glycogen phosphorylase activity which aligns with the Michaelis-Menten model of effector AMP. These results support the notion that Korean panax ginseng operates as an activator of Korean panax ginseng, thus increasing energy production through the catabolism of glycogen.

Mentor

Roberto De Guzman