The metal requirement of rat tyrosine hydroxylase

Research output: Contribution to journalArticle

55 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)211-215
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume161
Issue number1
DOIs
StatePublished - May 30 1989
Externally publishedYes

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Tyrosine 3-Monooxygenase
Rats
Iron
Metals
Enzyme activity
Enzymes
Nickel
Silver
Zinc
Copper
Atoms

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The metal requirement of rat tyrosine hydroxylase. / Fitzpatrick, Paul F.

In: Biochemical and Biophysical Research Communications, Vol. 161, No. 1, 30.05.1989, p. 211-215.

Research output: Contribution to journalArticle

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