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Biophysical Journal 55: 159-162 (1989)
© 1989 the Biophysical Society

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Radiation-damaged tyrosinase molecules are inactive.

E S Kempner and J H Miller

Laboratory of Physical Biology, National Institutes of Health, Bethesda, Maryland 20892.

ABSTRACT

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.






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Copyright © 1989 by the Biophysical Society.