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The metal requirement of rat tyrosine hydroxylase
1Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843.
Biochemical and Biophysical Research Communications
|May 30, 1989
Abstract:
The effect of added metals on purified rat tyrosine hydroxylase which is predominantly iron-free has been determined. The presence of 10 microM ferrous ammonium sulfate results in a ten-fold increase in the activity of enzyme containing 0.1 iron atom per subunit. The enzyme activity is half-maximal at a free ferrous iron concentration of 0.15 microM. Copper, zinc, silver, and nickel are unable to replace ferrous iron. Ferric iron is inactive unless ascorbate is included to reduce it.