rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
22
|
pubmed:dateCreated |
1984-1-7
|
pubmed:abstractText |
The activity of tyrosine hydroxylase (TH) in the corpus striatum of haloperidol treated and control rats has been examined. The activation of TH by haloperidol caused a decrease in the Km for tetrahydrobiopterin but no change in the Vmax. This effect was totally abolished when homogenates were prepared at high values of pH. A similar activation could be produced in vitro by preincubating with S-adenosylmethionine; conversely, enzyme activity was reduced by preincubating with S-adenosylhomocysteine. ATP and cyclic AMP activated the enzyme when incubated together with TH in vitro but the activity was reduced when the enzyme was preincubated with these substances. A possible role for carboxymethylation in controlling tyrosine hydroxylase activity is discussed.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0006-2952
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
32
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3369-74
|
pubmed:dateRevised |
2003-11-14
|
pubmed:meshHeading |
pubmed-meshheading:6140010-Adenosine Triphosphate,
pubmed-meshheading:6140010-Animals,
pubmed-meshheading:6140010-Corpus Striatum,
pubmed-meshheading:6140010-Cyclic AMP,
pubmed-meshheading:6140010-Enzyme Activation,
pubmed-meshheading:6140010-Haloperidol,
pubmed-meshheading:6140010-Homocysteine,
pubmed-meshheading:6140010-Hydrogen-Ion Concentration,
pubmed-meshheading:6140010-Kinetics,
pubmed-meshheading:6140010-Rats,
pubmed-meshheading:6140010-Rats, Inbred Strains,
pubmed-meshheading:6140010-S-Adenosylhomocysteine,
pubmed-meshheading:6140010-S-Adenosylmethionine,
pubmed-meshheading:6140010-Tyrosine 3-Monooxygenase
|
pubmed:year |
1983
|
pubmed:articleTitle |
Activation and inactivation of striatal tyrosine hydroxylase: the effects of pH, ATP and cyclic AMP, S-adenosylmethionine and S-adenosylhomocysteine.
|
pubmed:publicationType |
Journal Article
|