Abstract
Two monomeric tyrosinases were isolated from fruitbodies of Agaricus bisporus strain U1. Both tyrosinases, with pIs ca 5.2 and 5.1, showed an M r of ca 43 kDa under reducing and denaturing conditions and of ca 47 kDa under native conditions, and similar cresolase and catecholase activities of, respectively, 90–120 nkat mg −1 and 17–18 μkat mg −1. The enzyme preparations were >95% homogeneous. Neither isoform appeared to be glycosylated or phosphorylated. Upon purification the isoforms showed a gradual decrease in pI from ca 5.4–5.6 to ca 5.1–5.2.
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