BIOCHEMICAL-CHARACTERIZATION OF GLYCYRRHIZIN AS AN EFFECTIVE INHIBITOR FOR HYALURONIDASES FROM BOVINE TESTIS

The inhibitory effects of several anti-inflammatory agents, including glycyrrhizin (GL), on the activities of hyaluronidases (HAses) purifie d from bovine testes and Streptomyces were investigated in vitro. It w as found that (i) GL inhibits the activity of HAse (p55) from bovine t estes in a dose-dependent manner, but does not affect HAse from Strept omyces; (ii) GL was the most effective of the compounds tested on bovi ne testis HAse activity (50% inhibition with approx, 3 mu M GL); and ( iii) glycyrrhetinic acid (GA), a derivative (oGA) of GA and diglucuron ic acid had no detectable effects on HAse activity at 9.0 mu M. The GL -induced inhibition of HAse activity is uncompetitive for its substrat es. Data are provided to support the contentions that (i) bovine testi s HAse (p55) is a GL-binding protein; and (ii) GL acts as a potent inh ibitor of HAse in vitro.