| pubmed-article:1633830 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1633830 | lifeskim:mentions | umls-concept:C0015161 | lld:lifeskim |
| pubmed-article:1633830 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:1633830 | lifeskim:mentions | umls-concept:C0007407 | lld:lifeskim |
| pubmed-article:1633830 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:1633830 | lifeskim:mentions | umls-concept:C1882598 | lld:lifeskim |
| pubmed-article:1633830 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:1633830 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:1633830 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:1633830 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:1633830 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1633830 | pubmed:dateCreated | 1992-8-25 | lld:pubmed |
| pubmed-article:1633830 | pubmed:abstractText | The rat and human recombinant soluble and membrane-bound catechol O-methyltransferase (S- and MB-COMT, respectively) were expressed using mammalian and baculovirus vectors. Low levels of rat and human S-COMT polypeptides were detected by immunoprecipitation in K-562 cell lines transfected with the S-COMT vectors. From K-562 cells transfected with the rat MB-COMT construct, both S- and MB-COMT recombinant proteins were detected by a rat COMT-specific anti-serum. Infection of lepidopteran Spodoptera frugiperda cells with recombinant S- or MB-COMT baculovirus constructs yielded high amounts of enzymically active and immunoreactive S- or MB-COMT proteins, respectively. Pulse/chase experiments with [35S]methionine-labelled insect cells infected with the MB-COMT baculovirus showed that the 30-kDa recombinant human MB-COMT polypeptide was not processed into the 25-kDa S-COMT form. Subcellular fractionations of insect cells, followed by immunoblotting with COMT antiserum, showed that recombinant S-COMT was found only in the soluble, cytoplasmic fraction, whereas MB-COMT resided both in soluble and membrane fractions. The recombinant MB-COMT sedimented in Percoll gradients at the density of 1.042 g/ml cosedimenting with the plasma-membrane marker. Fractionation and immunoblotting experiments on homogenized total rat brains indicated that the rat S-COMT (24 kDa) and some of the rat MB-COMT (28 kDa) was recovered in soluble fractions, whereas the microsomal material having COMT activity contained the MB-COMT polypeptide. The rat brain microsomal MB-COMT had a density of 1.042 g/ml in Percoll gradients, cosedimenting with the plasma-membrane and rough-endoplasmic-reticulum marker enzymes. The meta/para methylation ratio of dihydroxybenzoic-acid substrate by different recombinant and rat brain COMT-containing subcellular fractions was analysed. | lld:pubmed |
| pubmed-article:1633830 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1633830 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1633830 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1633830 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1633830 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1633830 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1633830 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1633830 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1633830 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:1633830 | pubmed:author | pubmed-author:LundströmKK | lld:pubmed |
| pubmed-article:1633830 | pubmed:author | pubmed-author:KalkkinenNN | lld:pubmed |
| pubmed-article:1633830 | pubmed:author | pubmed-author:UlmanenII | lld:pubmed |
| pubmed-article:1633830 | pubmed:author | pubmed-author:JulkunenII | lld:pubmed |
| pubmed-article:1633830 | pubmed:author | pubmed-author:JalankoAA | lld:pubmed |
| pubmed-article:1633830 | pubmed:author | pubmed-author:TilgmannCC | lld:pubmed |
| pubmed-article:1633830 | pubmed:author | pubmed-author:MelenKK | lld:pubmed |
| pubmed-article:1633830 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1633830 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1633830 | pubmed:volume | 207 | lld:pubmed |
| pubmed-article:1633830 | pubmed:geneSymbol | COMT | lld:pubmed |
| pubmed-article:1633830 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1633830 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1633830 | pubmed:pagination | 813-21 | lld:pubmed |
| pubmed-article:1633830 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
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| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:meshHeading | pubmed-meshheading:1633830-... | lld:pubmed |
| pubmed-article:1633830 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1633830 | pubmed:articleTitle | Expression of recombinant soluble and membrane-bound catechol O-methyltransferase in eukaryotic cells and identification of the respective enzymes in rat brain. | lld:pubmed |
| pubmed-article:1633830 | pubmed:affiliation | Orion-Farmos Pharmaceuticals, Orion Research Center, Helsinki, Finland. | lld:pubmed |
| pubmed-article:1633830 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1633830 | pubmed:publicationType | In Vitro | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1633830 | lld:pubmed |
