Advisor(s)
Ronald Peterson, PhD
Ohio Northern University
Chemistry & Biochemistry, Science, Technology, and Mathematics
r-peterson@onu.edu
Document Type
Poster
Location
ONU McIntosh Center; Activities Room
Start Date
22-4-2022 10:00 AM
End Date
22-4-2022 11:00 AM
Abstract
In an academic setting, enzyme kinetics are introduced by analysis of the initial rates using the Michaelis-Menten model. To better understand enzyme kinetics, a complete time course analysis will provide a larger set of data, including information on feedback or product inhibition. With this, the Lambert W function can be used to analyze the integrated rate equations. We have started our analysis with the enzyme, acid phosphatase. Inorganic phosphorus is a known competitive inhibitor of the acid phosphatase catalyzed hydrolysis of p-nitrophenylphosphate. Using the integrated form of the rate equation allows us to determine the relative relationship of the Ki and Km. Analysis of the reaction by quantification of each product will allow for analysis of the inhibition mechanism by one or both of the products.
Recommended Citation
Gouge, Melissa, "Using Integrated Rate Equations to Analyze Acid Phosphatase Kinetics" (2022). ONU Student Research Colloquium. 17.
https://digitalcommons.onu.edu/student_research_colloquium/2022/posters/17
Using Integrated Rate Equations to Analyze Acid Phosphatase Kinetics
ONU McIntosh Center; Activities Room
In an academic setting, enzyme kinetics are introduced by analysis of the initial rates using the Michaelis-Menten model. To better understand enzyme kinetics, a complete time course analysis will provide a larger set of data, including information on feedback or product inhibition. With this, the Lambert W function can be used to analyze the integrated rate equations. We have started our analysis with the enzyme, acid phosphatase. Inorganic phosphorus is a known competitive inhibitor of the acid phosphatase catalyzed hydrolysis of p-nitrophenylphosphate. Using the integrated form of the rate equation allows us to determine the relative relationship of the Ki and Km. Analysis of the reaction by quantification of each product will allow for analysis of the inhibition mechanism by one or both of the products.