TY - JOUR
T1 - The metal requirement of rat tyrosine hydroxylase
AU - Fitzpatrick, Paul F.
N1 - Funding Information:
This work was supported in part by NIH Biomedical Research Support Grant RR07090, a grant from the Texas Advanced Research Project, and National Science Foundation Grant DMB-8816407.
PY - 1989/5/30
Y1 - 1989/5/30
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(89)91582-9
DO - 10.1016/0006-291X(89)91582-9
M3 - Article
C2 - 2567163
AN - SCOPUS:0024324003
VL - 161
SP - 211
EP - 215
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -