Abstract
The effect of added metals on purified rat tyrosine hydroxylase which is predominantly iron-free has been determined. The presence of 10 μM 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 μM. Copper, zinc, silver, and nickel are unable to replace ferrous iron. Ferric iron is inactive unless ascorbate is included to reduce it.
Original language | English (US) |
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Pages (from-to) | 211-215 |
Number of pages | 5 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 161 |
Issue number | 1 |
DOIs | |
State | Published - May 30 1989 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology