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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1989-2-9
|
| pubmed:abstractText |
Superoxide dismutase comprises a family of metalloenzymes that catalyze the oxido-reduction of superoxide anion to H2O2. Manganese superoxide dismutase (Mn-SOD) is encoded by nuclear chromatin, synthesized in the cytosol, and imported posttranslationally into the mitochondrial matrix. We isolated and sequenced complementary DNA encoding human Mn-SOD. The Mn-SOD cDNA was 1001 base pairs long with a single open reading frame. It contained 95 base pairs of 5' untranslated sequence, and 216 base pairs of 3' untranslated sequence, followed by a short polyadenylation tract. The deduced amino acid sequence suggests a mature protein of 198 amino acids preceded by a 24 amino acid leader peptide. A major transcript of 1000 nucleotides was identified by hybridization of the cDNA with RNA isolated from human cells. Precursor Mn-SOD was produced by in vitro transcription of the human Mn-SOD cDNA followed by in vitro translation utilizing rabbit reticulocyte lysate. The primary translation product of the cDNA is a polypeptide of Mr 26,000 as determined by sodium dodecyl sulfate-polyacrylamide electrophoresis. When the Mr 26,000 propeptide was incubated with freshly isolated rat liver mitochondria, the peptide was proteolytically processed to a Mr 24,000 polypeptide. Proteolytic processing was accompanied by an energy-dependent import of the peptide into the isolated liver mitochondria. Mature 125I-labelled Mn-SOD, isolated from rabbit liver, was not imported in vitro into mitochondria, indicating that the energy-dependent uptake of Mn-SOD by liver mitochondria was specific for the Mn-SOD precursor.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
19
|
| pubmed:volume |
994
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
30-6
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2462451-Amino Acid Sequence,
pubmed-meshheading:2462451-Animals,
pubmed-meshheading:2462451-Base Sequence,
pubmed-meshheading:2462451-Blotting, Northern,
pubmed-meshheading:2462451-Carcinoma, Hepatocellular,
pubmed-meshheading:2462451-DNA,
pubmed-meshheading:2462451-Liver,
pubmed-meshheading:2462451-Liver Neoplasms,
pubmed-meshheading:2462451-Lung,
pubmed-meshheading:2462451-Manganese,
pubmed-meshheading:2462451-Mitochondria, Liver,
pubmed-meshheading:2462451-Molecular Sequence Data,
pubmed-meshheading:2462451-Molecular Weight,
pubmed-meshheading:2462451-Protein Biosynthesis,
pubmed-meshheading:2462451-Protein Precursors,
pubmed-meshheading:2462451-RNA,
pubmed-meshheading:2462451-RNA, Messenger,
pubmed-meshheading:2462451-Rabbits,
pubmed-meshheading:2462451-Rats,
pubmed-meshheading:2462451-Superoxide Dismutase
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Synthesis and processing of the precursor for human mangano-superoxide dismutase.
|
| pubmed:affiliation |
Department of Pediatrics, University of Cincinnati, OH 45267-0541.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|