Abstract
Summary
1. Protyrosinase from the egg of the grasshopper, Melanoplus differentialis was activated to form tyrosinase by the following reagents: sodium dioctyl sulfosuccinate (aerosol OT), sodium dodecyl sulfate, HgCl2, heat (70°-10'), and urea. 2. Tyrosinase, produced by different activators, was allowed to act upon monohydric (tyramine-HCl, p-cresol) and o-dihydric (catechol) phenols as substrates and relative rates of activity studied. 3. All enzymes tested showed activity for both monohydric and o-dihydric phenols. 4. Urea and HgCl2 activated tyrosinase showed high monophenolase activity and low catecholase activity. All other enzyme samples exhibited both monophenolase and catecholase activity in varying degrees. 5. Animal and plant tyrosinases seem similar in that both possess enzymatic activities more or less conditioned by chemical treatments.
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