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Tyrosine hydroxylase: studies on the phosphorylation of a purified preparation of the brain enzyme by the cyclic AMP-dependent protein kinase

AM Edelman, JD Raese, MA Lazar and JD Barchas

Tyrosine hydroxylase [L-tyrosine, tetrahydropteridine: oxygen oxidoreductase (3-hydroxylating); EC 1.14.16.2](TH) was purified from bovine corpus striatum. The purification involved sequential DEAE cellulose, hydroxylapatite and CM Sephadex C-50 chromatography, followed by glycerol density gradient centrifugation. Final preparations appeared to be 90 to 100% pure as judged by polyacrylamide gel electrophoresis under denaturing conditions in acetic acid-urea. The enzyme was estimated to have a minimum molecular weight of approximately 60,000 daltons. Purified TH could be activated in vitro by incubation with magnesium adenosine triphosphate and the catalytic subunit of cyclic AMP-dependent protein kinase (ATP/protein phosphotransferase; EC 2.7.1.37). When the final purified preparation of TH was incubated under these conditions utilizing [gamma-32P]ATP, it was found to incorporate 0.7 to 0.9 mol of phosphorus/mol of protein. These results suggest that the activation of TH in the presence of phosphorylating conditions is due to its phosphorylation by cyclic AMP- dependent protein kinase.

Volume 216, Issue 3, pp. 647-653, 03/01/1981
Copyright © 1981 by American Society for Pharmacology and Experimental Therapeutics




This article has been cited by other articles:


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 J. Neurosci.Home page
Z. Guo, X. Du, and L. Iacovitti
Regulation of Tyrosine Hydroxylase Gene Expression during Transdifferentiation of Striatal Neurons: Changes in Transcription Factors Binding the AP-1 Site
J. Neurosci., October 15, 1998; 18(20): 8163 - 8174.
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