Απομόνωση και χαρακτηρισμός των πολυπεπτιδίων προθυμοσίνη α και παραθυμοσίνη από ιστούς χοίρου (Sus scrofa) (Doctoral thesis)

Οικονόμου, Μιχαήλ Σ.

ΡARATHYMOSIN A, A HIGHLY ACIDIC POLYPEPTIDE, HAS BEEN ISOLATED AND CHARACTERIZED FROM PORCINE THYMUS, SPLEEN, LUNG, KIDNEY AND LIVER. IN ADDITION THE RELATED ACIDIC POLYPEPTIDE PARATHYMOSIN HAS BEEN ISOLATED AND CHARACTERIZED FROM PORCINE LIVER. PORCINE PROTHYMOSINE A CONTAINS 109 AMINOACIDS (MW 12,050). IT LACKS AROMATIC AND SULFUR CONTAINING AMINO ACIDS AND HAS A HIGH CONTENT OF GLUTAMIC AND ASPARTIC ACID. PARATHYMOSIN WAS ISOLATED FROM PIG LIVER. PARATHYMOSIN HAS STRUCTURAL HOMOLOGY TO PROTHYMOSIN A, CONTAINS 101 AMINO ACIDS, IS HIGHLY ACIDIC AND LACKS AROMATIC AND SULFUR CONTAINING AMINO ACIDS. A SENSITIVE AND SPECIFIC COMPETITION MICRO ELISA ASSAY HAS BEEN DEVELOPED FOR THE ASSAY OFPARATHYMOSIN IN TISSUE EXTRACTS. NON-LYMPHOID TISSUES TO BE RICHER IN PARATHYMOSIN COMPARED WITH PROTHYMOSIN A. THE SECONDARY STRUCTURE OF PROTHYMOSIN A AND PARATHYMOSIN HAVE BEEN INVESTIGATED BY MEANS OF CIRCULAR DICHROIC (CD) SPECTROSCOPY IN THE FAR ULTRAVIOLET RANGE OF 200-260NM. THE PEPTIDES WERE FOUNDTO HAVE RANDOM COIL STRUCTURES AT PHYSIOLOGICAL AND ACIDIC PH IN PBS.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων Σχολή Θετικών Επιστημών Τμήμα Χημείας
Subject classification: Πεπτίδια
Keywords: Θυμοσίνες,Όξινα πολυπεπτίδια,Παραθυμοσίνη,Προθυμοσίνη α,Πυρηνικές πρωτεΐνες
URI: https://olympias.lib.uoi.gr/jspui/handle/123456789/771
http://dx.doi.org/10.26268/heal.uoi.768
Link: http://thesis.ekt.gr/thesisBookReader/id/3647#page/1/mode/2up
Appears in Collections:Διδακτορικές Διατριβές

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