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 › peer-review

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

Access to Document

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

Fingerprint Dive into the research topics of 'The metal requirement of rat tyrosine hydroxylase'. Together they form a unique fingerprint.

Cite this

@article{bbf7a66e4af049e48d1e4330639e9f87,

title = "The metal requirement of rat tyrosine hydroxylase",

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.",

author = "Fitzpatrick, {Paul F.}",

year = "1989",

month = may,

day = "30",

doi = "10.1016/0006-291X(89)91582-9",

language = "English (US)",

volume = "161",

pages = "211--215",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "1",

}

TY - JOUR

T1 - The metal requirement of rat tyrosine hydroxylase

AU - Fitzpatrick, Paul F.

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.

UR - http://www.scopus.com/inward/record.url?scp=0024324003&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024324003&partnerID=8YFLogxK

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 -