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https://olympias.lib.uoi.gr/jspui/handle/123456789/22532Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Clinton, M. | en |
| dc.contributor.author | Frangou-Lazaridis, M. | en |
| dc.contributor.author | Panneerselvam, C. | en |
| dc.contributor.author | Horecker, B. L. | en |
| dc.date.accessioned | 2015-11-24T19:24:50Z | - |
| dc.date.available | 2015-11-24T19:24:50Z | - |
| dc.identifier.issn | 0006-291X | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/22532 | - |
| dc.rights | Default Licence | - |
| dc.subject | Amino Acid Sequence | en |
| dc.subject | Animals | en |
| dc.subject | Base Sequence | en |
| dc.subject | *Cloning, Molecular | en |
| dc.subject | Codon | en |
| dc.subject | DNA/*genetics/isolation & purification | en |
| dc.subject | DNA Probes | en |
| dc.subject | DNA Restriction Enzymes | en |
| dc.subject | Electrophoresis, Agar Gel | en |
| dc.subject | Humans | en |
| dc.subject | Kidney/*analysis | en |
| dc.subject | Molecular Sequence Data | en |
| dc.subject | Nucleic Acid Hybridization | en |
| dc.subject | Rats | en |
| dc.subject | Sequence Homology, Nucleic Acid | en |
| dc.subject | Thymosin/*analogs & derivatives/genetics | en |
| dc.title | The sequence of human parathymosin deduced from a cloned human kidney cDNA | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/2537638 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/0006291X89928015/1-s2.0-0006291X89928015-main.pdf?_tid=c7913907e35b836cf11524d752e23c51&acdnat=1332915369_11b4b6d91550bbb5672ac6add56b05bc | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 1989 | - |
| heal.abstract | The amino acid sequence of human parathymosin has been deduced from the cDNA sequence of a clone isolated from a human kidney cDNA library. Screening of the cDNA library with a probe containing a partial rat cDNA sequence yielded two clones containing inserts of 1200 and 1100 base pairs respectively, each including the complete open reading frame for human parathymosin. The open reading frame contains 306 nucleotides, including the codon for the initiator methionine. Analysis of the 5' flanking sequence excluded the presence of a hydrophobic signal peptide in the translated sequence. It may therefore be concluded that parathymosin, like prothymosin alpha, is synthesized without formation of a large precursor polypeptide. Comparison of the deduced amino acid sequence with the known primary structure of rat and bovine parathymosins shows that the primary structure of parathymosin is highly conserved among these species. | en |
| heal.journalName | Biochem Biophys Res Commun | en |
| heal.journalType | peer-reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Clinton-1989-The sequence of huma.pdf | 524.75 kB | Adobe PDF | View/Open Request a copy |
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