Thermal Denaturation of Native Striatal Tyrosine Hydroxylase: Increased Thermolability of the Phosphorylated Form of the Enzyme
- 1 February 1981
- journal article
- research article
- Published by Wiley in Journal of Neurochemistry
- Vol. 36 (2) , 677-682
- https://doi.org/10.1111/j.1471-4159.1981.tb01641.x
Abstract
Tyrosine hydroxylase was purified from bovine corpus striatum. The native enzyme had a half-life of 15 .+-. 3 min at 50.degree. 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.degree. C. Thermal denaturation studies indicated that phosphorylated tyrosine hydroxylase had a half-life of 5 .+-. 2 min at 50.degree. C.Keywords
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