Abstract
A new analysis method for protein phosphatase type 2A inhibitors was established that uses the firefly bioluminescence system for detection. Thus, firefly luciferin phosphate was used as a substrate, and the liberated free luciferin was determined from the amount of light emitted from the immobilized luciferase. This method was successfully used to determine the activities of known inhibitors, i.e., okadaic acid, calyculin A, microcystin-LR and tautomycin using less than 10 pmol of a sample.
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