Abstract
Rat kidney homogenate incubated with trypsin reduced the activity of β-glucuronidase. Since the incubated trypsin-solution without the homogenate showed no influence on the activity of β-glucuronidase, it was concuded that a certain inhibitor of the enzyme was turned out in rat kid ey tissue by trypsin treatment. A cortex fraction proved to be more effective than a medulla fraction, and among celluler components, a soluble fractioh was most potent.Furthermore, an addition of sodium sulfate not only abolished the inhibitory effect caused by the trypsin treatment but also activated β-glucuronidase to a certain level.This fact suggests that sodium sulfate is not a mere activator, but an agent having an ability to release the inhibitors from β-glucuronidase.
