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Leukocyte esterase

Test for white blood cells in urine

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  • 2 chapters

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Through Infection

Structure and function

In a study using cytochemical methods and polyacrylamide gel electrophoresis, nine different esterase isozymes have been identified in human leukocytes with somewhat varying substrate specificities.

Esterase enzymes have the activity of hydrolyzing ester bonds in various substrates. In an electrochemical study using an ester substrate called 4-((tosyl-l-alanyl)oxy)phenyl tosyl-l-alaninate (TAPTA), direct esterolytic activity of leukocyte esterase could be demonstrated. Leukocyte esterase was found to hydrolyze TAPTA, releasing a redox-active fragment that provided a numerical measure of leukocyte esterase activity when oxidized at an electrode.

Studies on the direct immune function of leukocyte esterase activity, however, are unclear. Although leukocyte esterase is released by neutrophils in response to infection, there is limited research on its direct role in the degradation of pathogens or foreign substances during phagocytosis by neutrophils. Instead, leukocyte esterase serves more as an indicator of an immune response, as it reflects the presence of active white blood cells.

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