Monovalent Cations and Striatal Tyrosine Hydroxylase
- 1 September 1982
- journal article
- research article
- Published by Wiley in Journal of Neurochemistry
- Vol. 37 (3), 681-686
- https://doi.org/10.1111/j.1471-4159.1982.tb12541.x
Abstract
The kinetic properties of soluble tyrosine hydroxylase [EC 1.14.16.2] from rat striatum and the activation of the enzyme by the polyanion heparin were assessed as a function of the monovalent cations K+, Na+, tetramethylammonium (TMA+) and Tris. Substitution of K+ or Na+ for TMA+ or Tris can alter the kinetic properties of tyrosine hydroxylase in the absence of heparin, the nature of the interaction of the enzyme with heparin, and also the kinetic properties of the heparin-activated enzyme. Monovalent cations can probably support unique conformational states of the enzyme.Keywords
This publication has 11 references indexed in Scilit:
- Physical state of tyrosine hydroxylase in the ganglia and nerve endingsGeneral Pharmacology: The Vascular System, 1979
- Tyrosine hydroxylase:—Examination of conditions influencing activity in pheochromocytoma, adrenal medulla and striatumBiochemical Pharmacology, 1979
- Activation of tyrosine hydroxylase by polyanions and salts An electrostatic effectBiochimica et Biophysica Acta (BBA) - Enzymology, 1976
- The stimulation of partially purified bovine caudate tyrosine hydroxylase by phosphatidyl-L-serineBiochemical and Biophysical Research Communications, 1974
- Effect of sodium dodecyl sulfate on the kinetic properties and molecular weight of rat striatal tyrosine hydroxylaseLife Sciences, 1974
- Regulatory Properties of Soluble and Particulate Rat Brain Tyrosine HydroxylaseJournal of Biological Chemistry, 1972
- Interactions of fructose 1,6-diphosphate, substrates, and monovalent cations with yeast pyruvate kinase monitored by changes in enzyme fluorescenceBiochemistry, 1971
- Role of Mineral Elements with Emphasis on the Univalent CationsAnnual Review of Plant Physiology, 1966
- A rapid and simple radioassay for tyrosine hydroxylase activityAnalytical Biochemistry, 1964
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951