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Subject | Predicate | Object |
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http://purl.uniprot.org/citations/8308018 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/8308018 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/8308018 | http://www.w3.org/2000/01/rdf-schema#comment | "Adenylosuccinate synthetase (EC 6.3.4.4) catalyzes the initial step in the conversion of IMP to AMP. Two isoforms of this enzyme have been observed in vertebrates. A muscle isozyme is highly abundant in cardiac and skeletal muscle tissue and is thought to play a role in muscle energy metabolism. The non-muscle isozyme, which is present at low levels in most tissues, likely functions in de novo AMP biosynthesis. The analysis of the non-muscle isozyme has been hampered by its low abundance and instability during purification. In this study a genetic selection scheme was used to generate a murine T-lymphoma cell line which was at least 100-fold enriched for the non-muscle isozyme, as a result of amplification of the non-muscle synthetase gene. This cell line made possible the purification of the non-muscle isozyme, and the subsequent isolation of isozyme-specific peptides. Based on peptide sequence information a degenerate oligonucleotide probe was designed and used to screen a mouse kidney cDNA library. A 1.5-kilobase cDNA encoding the non-muscle isozyme was cloned and found to contain an open reading frame of 1368 base pairs encoding 456 amino acids. Gene transfer experiments showed that the cDNA encoded a 50-kDa protein, the size expected for mammalian synthetases, that correlated with the presence of high levels of synthetase activity. The deduced amino acid sequence of the mouse non-muscle synthetase is approximately 75% identical to the previously reported mouse muscle synthetase. Southern blot analysis of mouse genomic DNA with the isozyme-specific cDNA probes revealed that the synthetase isozymes are encoded by separate genes. The non-muscle gene is expressed in most tissues but is virtually undetectable in striated muscle tissues. Three different transcripts (1.7, 2.8, and 3.4 kilobases) are detected for the non-muscle isozyme which show a similar tissue distribution. The availability of a cDNA for the non-muscle isozyme of adenylosuccinate synthetase will facilitate further comparative analyses with the previously cloned muscle isozyme."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(17)41805-9"xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(17)41805-9"xsd:string |
http://purl.uniprot.org/citations/8308018 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8308018 |
http://purl.uniprot.org/citations/8308018 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8308018 |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/author | "Rudolph F.B."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/author | "Rudolph F.B."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/author | "Kellems R.E."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/author | "Kellems R.E."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/author | "Cooper B.F."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/author | "Cooper B.F."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/author | "Guicherit O.M."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/author | "Guicherit O.M."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/pages | "4488-4496"xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/pages | "4488-4496"xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/title | "Amplification of an adenylosuccinate synthetase gene in alanosine-resistant murine T-lymphoma cells. Molecular cloning of a cDNA encoding the 'non-muscle' isozyme."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/title | "Amplification of an adenylosuccinate synthetase gene in alanosine-resistant murine T-lymphoma cells. Molecular cloning of a cDNA encoding the 'non-muscle' isozyme."xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/volume | "269"xsd:string |
http://purl.uniprot.org/citations/8308018 | http://purl.uniprot.org/core/volume | "269"xsd:string |