Abstract
Abstract: Tyrosine hydroxylase purified from rat pheochro‐mocytoma was phosphorylated and activated by purified cyclic GMP‐dependent protein kinase as well as by cyclic AMP‐dependent protein kinase catalytic subunit. The extent of activation was correlated with the degree of phosphate incorporated into the enzyme. Comparable stoichio‐metric ratios (0.6 mol phosphate/mol tyrosine hydroxylase subunit) were obtained at maximal concentrations of either cyclic AMP‐dependent or cyclic GMP‐dependent protein kinases. The enzymes appeared to mediate the phosphorylation of the same residue based on the observation that incorporation was not increased when both enzymes were present. The major tryptic phosphopeptide obtained from tyrosine hydroxylase phosphorylated by each protein kinase exhibited an identical retention time following HPLC. The purified phosphopeptides also exhibited identical isoelectric points. These data provide support for the notion that the protein kinases are phosphorylating the same residue of tyrosine hydroxylase.
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Dates
Type | When |
---|---|
Created | 18 years, 11 months ago (Oct. 5, 2006, 4 p.m.) |
Deposited | 1 year, 10 months ago (Oct. 21, 2023, 8:09 a.m.) |
Indexed | 1 year, 3 months ago (May 13, 2024, 11:11 p.m.) |
Issued | 38 years, 6 months ago (March 1, 1987) |
Published | 38 years, 6 months ago (March 1, 1987) |
Published Online | 18 years, 11 months ago (Oct. 5, 2006) |
Published Print | 38 years, 6 months ago (March 1, 1987) |
@article{Roskoski_1987, title={Phosphorylation of Tyrosine Hydroxylase by Cyclic GMP‐Dependent Protein Kinase}, volume={48}, ISSN={1471-4159}, url={http://dx.doi.org/10.1111/j.1471-4159.1987.tb05593.x}, DOI={10.1111/j.1471-4159.1987.tb05593.x}, number={3}, journal={Journal of Neurochemistry}, publisher={Wiley}, author={Roskoski, Robert and Vulliet, P. Richard and Glass, David B.}, year={1987}, month=mar, pages={840–845} }