Tyrosine Hydroxylase Purification from Rat PC 12 Cells
作者： Laura G. Gahn , Robert Roskoski
DOI: 10.1016/1046-5928(91)90002-Z
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摘要: Abstract Tyrosine hydroxylase was purified in high yield from rat PC 12 cells. This three-day procedure consisted of differential ammonium sulfate precipitation, anion-exchange chromatography, and heparin-Sepharose affinity chromatography. It yielded an average 15 mg protein 100 flasks PC12 cells, with greater than 40% recovery tyrosine hydroxylase. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis a single band molecular weight approximately 60,000. The had specific activity 670 nmol/min/mg K m for its reducing cofactor tetrahydrobiopterin 1.8 mm. can be phosphorylated activated by cyclic AMP-dependent kinase.
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