Please use this identifier to cite or link to this item:
https://olympias.lib.uoi.gr/jspui/handle/123456789/22411Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Haritos, A. A. | en |
| dc.contributor.author | Tsolas, O. | en |
| dc.contributor.author | Horecker, B. L. | en |
| dc.date.accessioned | 2015-11-24T19:24:04Z | - |
| dc.date.available | 2015-11-24T19:24:04Z | - |
| dc.identifier.issn | 0027-8424 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/22411 | - |
| dc.rights | Default Licence | - |
| dc.subject | Amino Acids/analysis | en |
| dc.subject | Animals | en |
| dc.subject | Brain Chemistry | en |
| dc.subject | Kidney/analysis | en |
| dc.subject | Liver/analysis | en |
| dc.subject | Lung/analysis | en |
| dc.subject | Protein Precursors/*analysis | en |
| dc.subject | Radioimmunoassay/methods | en |
| dc.subject | Rats | en |
| dc.subject | Spleen/analysis | en |
| dc.subject | Thymosin/*analogs & derivatives/analysis | en |
| dc.subject | Thymus Gland/*analysis | en |
| dc.subject | Tissue Distribution | en |
| dc.title | Distribution of prothymosin alpha in rat tissues | 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/6584887 | - |
| heal.identifier.secondary | http://www.pnas.org/content/81/5/1391.full.pdf | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 1984 | - |
| heal.abstract | A radioimmunoassay, using a rabbit antiserum directed against thymosin alpha 1, was employed to detect the presence of crossreacting peptides in rat tissues. Highest concentrations were present in thymus, but thymosin alpha 1 cross-reacting material was also detected in brain, liver, kidney, lung, and spleen, in amounts ranging from 15% to 65% of the quantities found in thymus. In each case, the major immunoreactive peptide, after extraction and purification by a procedure that avoids proteolytic modification, was identified as prothymosin alpha, a peptide containing approximately equal to 112 amino acid residues. Prothymosin alpha is believed to be the endogenous peptide from which thymosin alpha 1 and other fragments are formed by proteolytic modification during the preparation of thymosin fraction 5. No peptides corresponding in size and chromatographic behavior to thymosin alpha 1 were detected with the extraction procedure employed. | en |
| heal.journalName | Proc Natl Acad Sci U S A | 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 | |
|---|---|---|---|---|
| Haritos-1984-Distribution of prot.pdf | 619.3 kB | Adobe PDF | View/Open |
This item is licensed under a Creative Commons License
