Changes in the cofactor binding domain of bovine striatal tyrosine hydroxylase at physiological pH upon cAMP-dependent phosphorylation mapped with tetrahydrobiopterin analogues
- 24 January 1989
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 28 (2) , 494-504
- https://doi.org/10.1021/bi00428a013
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 5 references indexed in Scilit:
- Lipophilic 5,6,7,8-tetrahydropterin substrates for phenylalanine hydroxylase (monkey brain), tryptophan hydroxylase (rat brain) and tyrosine hydroxylase (rat brain)European Journal of Medicinal Chemistry, 1987
- Two forms of striatal tyrosine hydroxylase from DEAE-cellulose chromatographyBrain Research, 1983
- Dephosphorylation of purified brain tyrosine hydroxylase by rat striatal extractsNeurochemistry International, 1983
- Tyrosine hydroxylase: a substrate of cyclic AMP-dependent protein kinase.Proceedings of the National Academy of Sciences, 1980
- ATP, cyclic AMP, and magnesium increase the affinity of rat striatal tyrosine hydroxylase for its cofactor.Proceedings of the National Academy of Sciences, 1975