The metal requirement of rat tyrosine hydroxylase

Paul F. Fitzpatrick

doi:10.1016/0006-291X(89)91582-9

The metal requirement of rat tyrosine hydroxylase

Paul F. Fitzpatrick

Biochemistry & Structural Biology

Research output: Contribution to journal › Article

55 Scopus citations

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)
Pages (from-to)	211-215
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	161
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(89)91582-9
State	Published - May 30 1989

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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Fitzpatrick, P. F. (1989). The metal requirement of rat tyrosine hydroxylase. Biochemical and Biophysical Research Communications, 161(1), 211-215. https://doi.org/10.1016/0006-291X(89)91582-9

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