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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1995-5-23
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pubmed:abstractText |
A synthetic peptide corresponding to residues 32-47 of rat tyrosine hydroxylase (TH) was phosphorylated by protein kinase A at Ser40 and used to generate antibodies in rabbits. Reactivity of the anti-pTH32-47 antibodies with phospho- and dephospho-Ser40 forms of TH protein and peptide TH32-47 was compared with reactivity of antibodies to nonphosphorylated peptide and to native TH protein. In antibody-capture ELISAs, anti-pTH32-47 was more reactive with the phospho-TH than with the dephospho-TH forms. Conversely, antibodies against the nonphosphorylated peptide reacted preferentially with the dephospho-TH forms. In western blots, labeling of the approximately 60-kDa TH band by anti-pTH32-47 was readily detectable in lanes containing protein kinase A-phosphorylated native TH at 10-100 ng/lane. In blots of supernatants prepared from striatal synaptosomes, addition of a phosphatase inhibitor was necessary to discern labeling of the TH band with anti-pTH32-47. Similarly, anti-pTH32-47 failed to immunoprecipitate TH activity from supernatants prepared from untreated tissues, whereas prior treatment with either 8-bromoadenosine 3',5'-cyclic monophosphate or forskolin enabled removal of TH activity by anti-pTH32-47. Lastly, in immunohistochemical studies, anti-pTH32-47 selectively labeled catecholaminergic cells in tissue sections from perfusion-fixed rat brain.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/8-Bromo Cyclic Adenosine...,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Forskolin,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-3042
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
64
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2281-7
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7722513-8-Bromo Cyclic Adenosine Monophosphate,
pubmed-meshheading:7722513-Animals,
pubmed-meshheading:7722513-Antibodies,
pubmed-meshheading:7722513-Antibody Specificity,
pubmed-meshheading:7722513-Corpus Striatum,
pubmed-meshheading:7722513-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:7722513-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:7722513-Forskolin,
pubmed-meshheading:7722513-Immunoblotting,
pubmed-meshheading:7722513-Immunohistochemistry,
pubmed-meshheading:7722513-Immunosorbent Techniques,
pubmed-meshheading:7722513-Male,
pubmed-meshheading:7722513-PC12 Cells,
pubmed-meshheading:7722513-Phosphorylation,
pubmed-meshheading:7722513-Phosphoserine,
pubmed-meshheading:7722513-Rats,
pubmed-meshheading:7722513-Rats, Sprague-Dawley,
pubmed-meshheading:7722513-Recombinant Proteins,
pubmed-meshheading:7722513-Synaptosomes,
pubmed-meshheading:7722513-Tyrosine 3-Monooxygenase
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pubmed:year |
1995
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pubmed:articleTitle |
Antibodies to a segment of tyrosine hydroxylase phosphorylated at serine 40.
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pubmed:affiliation |
Neurochemistry Research Laboratories, New York University Medical Center, NY 10016, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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