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. 1981 Feb;36(2):677-82.
doi: 10.1111/j.1471-4159.1981.tb01641.x.

Thermal denaturation of native striatal tyrosine hydroxylase: increased thermolability of the phosphorylated form of the enzyme

M A Lazar, R J Truscott, J D Raese, J D Barchas

Thermal denaturation of native striatal tyrosine hydroxylase: increased thermolability of the phosphorylated form of the enzyme

M A Lazar et al. J Neurochem. 1981 Feb.

Abstract

Tyrosine hydroxylase was purified from bovine corpus striatum. The native enzyme had a half-life of 15 +/- 3 min at 50 degrees C. Phosphorylation of tyrosine hydroxylase with protein kinase purified from both corpus striatum and heart activated the enzyme, but activity was rapidly lost with additional preincubation of the enzyme at 30 degrees C. Thermal denaturation studies indicated that phosphorylated tyrosine hydroxylase had a half-life of 5 +/- 2 min at 50 degrees C

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