Abstract
A new method of directly measuring esterase activity within phagolysosomes has been developed. Decanoyl fluorescein- binding microspheres were prepared and phagocytosed by human peripheral neutrophils. Within phagolysosomes lysosomal esterase hydrolyzed decanoyl fluorescein on the microspheres, causing the conversion of decanoyl fluorescein- binding microspheres (non-fluorescent) into fluorescein- binding microspheres (fluorescent). The activity of phagolysosomal esterase in intact neutrophils was assayed by the measurement of the fluorescence intensity without rupturing cells. By use of a flow cytometer, esterase activity within phagolysosomes in single cells was measured.
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