INCREASE IN RAT BRAIN TYROSINE HYDROXYLASE ACTIVITY PRODUCED BY ELECTROCONVULSIVE SHOCK
نویسندگان
چکیده
منابع مشابه
Tyrosine hydroxylase activity and extrinsic fluorescence changes produced by polyanions.
The activity of tyrosine hydroxylase in vitro is affected by many factors, including pH, phosphorylation by several protein kinases, and polyanions. We investigated the activation of tyrosine hydroxylase by RNA or DNA (polyanions), using purified rat PC12 cell enzyme. RNA and DNA each increased tyrosine hydroxylase activity in the presence of subsaturating (125 microM) tetrahydrobiopterin at pH...
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Tyrosine hydroxylase (TH) was purified from bovine brain and enzymatically phosphorylated in vitro. Radioactively phosphorylated TH was dephosphorylated by rat tissue extracts. Of tissues examined, rat corpus striatal extracts were highest in specific activity in the TH dephosphorylating assay. Phosphorylated histone did not inhibit dephosphorylation of TH by rat striatal extracts. The thermal ...
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Rat brain tyrosine hydroxylase exists in two distinct physical forms, a soluble and a membrane-bound form, The two forms are brain-region specific, with the membranebound or particulate form predominating in the striatum, an area enriched in catecholamine nerve endings and associated with a specific membrane fraction. Whereas the soluble and the particulate enzymes exhibit an identical Km for t...
متن کاملInactivation of phosphorylated rat tyrosine hydroxylase by ascorbate in vitro.
Tyrosine hydroxylase activity is reversibly controlled by the actions of several protein kinases. Previous studies showed that, following phosphorylation by protein kinase A, physiological concentrations of ascorbate irreversibly inactivate tyrosine hydroxylase. Several studies were performed to establish the mechanism of inactivation. We found that inactivation occurred under oxygen-free condi...
متن کاملActivation by cyclic 3':5'-adenosine monophosphate of tyrosine hydroxylase in the rat brain.
Membrane-permeable derivatives of cyclic AMP (cAMP) produced concentration-dependent increases in activity of tyrosine hydroxylase (L-tyrosine, tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14.16.2) in membrane-limited nerve endings (synaptosomes) prepared from three regions of rat brain. Increased hydroxylation occurred even after preincubation and removal of dibutyryl cycl...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1969
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.63.4.1117