What is the primary biochemical method for measuring enzyme activity?

The primary biochemical method for measuring enzyme activity is spectrophotometry. This technique is widely used because it allows for the quantitative measurement of the concentration of substances based on the absorption of light at specific wavelengths. When enzymes catalyze a reaction, they often lead to the production or consumption of colored compounds or changes in light absorbance. By measuring the change in absorbance over time, researchers can determine the rate of the enzymatic reaction, which directly reflects the enzyme's activity.

Spectrophotometry is favored in clinical laboratories due to its simplicity, rapid results, and ability to assess multiple samples simultaneously. It is particularly useful for enzymes that produce or degrade substrates in a way that results in measurable optical changes, making it a staple method for enzyme activity assays in various biochemical and clinical settings.

While other methods like chromatography, electrophoresis, and mass spectrometry can provide valuable information about enzymes and their properties, they are not primarily designed for real-time measurement of enzyme activity. Chromatography separates components of mixtures, electrophoresis focuses on the movement of proteins in a gel, and mass spectrometry identifies the mass-to-charge ratio of ions. These techniques may be used as complementary methods but do not serve as the primary approach for assessing enzymatic