Related Experiment Video
Updated: Feb 5, 2026

Kinetic Measurement and Real Time Visualization of Somatic Reprogramming
Published on: July 30, 2016
Kinetic Measurement of Serpin Inhibitory Activity by Real-Time Fluorogenic Biochemical Assay
Jordan R Yaron1, Sriram Ambadapadi2, Liqiang Zhang2
1Center for Personalized Diagnostics, Biodesign Institute, Arizona State University, Tempe, AZ, USA. jyaron@asu.edu.
Abstract:
Biochemical fluorogenic and chromogenic assays facilitate real-time study of enzyme function. Based on the principle of enzymatic inhibition, these kinetic assays can be adapted to measure the function of serpins. Compared to traditional, electrophoretic study of serpin inhibitory complex formation, kinetic assays allow for finer temporal resolution as well as more quantitative comparisons between different conditions. This chapter describes methodology for performing real-time, kinetic measurement of serpin inhibitory activity by fluorogenic substrate conversion assay. Specifically, the methods covered include measurement of alpha-1-antitrypsin inhibitory activity against trypsin and heparin-dependent anti-thrombin III inhibitory activity against thrombin. These methods are scalable to small-volume, high-density format and can be applied for high-throughput screening of serpin activity modulators.
Related Concept Videos
Real Time RT-PCR
The real-time quantification of the number of amplified products is...
Kinetic Energy
Enzyme Kinetics
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Kinetic Molecular Theory: Molecular Velocities, Temperature, and Kinetic Energy
Excitatory and Inhibitory Effects of Neurotransmitters
Kinetic Friction

