| Title of Work: |
Determination of the Kinetic Parameters of Alkaline Phosphatase |
| Presenters, Majors: |
Spencer Wagner, Biology
Jason Kunz, Biology |
Abstract: Alkaline phosphatase is an enzyme that removes phosphate groups from many types of molecules, including nucleotides and proteins. This process is termed dephosphorylation. In this study, alkaline phosphatase will be characterized under steady-state kinetics. Studies under these conditions allow the determination of the kinetic parameters: Km, Vmax, and inhibition constants for inhibitors. These parameters provide important information about how enzymes respond to substrates and inhibitors. This information allows for the comparison of the enzyme’s kinetic properties to those of other enzymes, which catalyze similar reactions. Kinetic inhibition studies are important for evaluating the efficiency of pharmaceutical inhibitors as well as their mode of action on enzymes. In this study, a model substrate, p-nitrophenol phosphate is used to determine alkaline phosphatase’s Km, and Vmax. The inhibition, by one of its products, phosphate, is also investigated. |