Radiation-damaged tyrosinase molecules are inactive.
Target analysis of radiation inactivation of mushroom tyrosinase yields different target sizes for diphenoloxidase and monophenoloxidase activities, which correspond to the subunits H and HL2 (or HL), respectively. After gel electrophoresis of irradiated samples, all diphenoloxidase activity is observed at the same position as seen in the original material. Radiolytic fragments contain no detectable activity, consistent with a fundamental assumption of target theory.
Kempner
E S
ES
Laboratory of Physical Biology, National Institutes of Health, Bethesda, Maryland 20892.
Miller
J H
JH
D000364:Agaricus / Q000201:enzymology; D004156:Catechol Oxidase / Q000528:radiation effects*; D004307:Dose-Response Relationship, Radiation; D005615:Freezing; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors / Q000528:radiation effects*
D046911:Macromolecular Substances; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase