NR ATJO
AU Pucci,A.; Russo,F.; D'Acqui,L.; Rao,M.A.; Calamai,L.; Gianfreda,L.
TI Protection of recombinant Prion protein (recPrP) from oxidation by Low temperature Ashing (LTA) resulting from its adsorption and/or co-polymerized in synthetic humic-like complexes
QU International Conference - Prion 2005: Between fundamentals and society's needs - 19.10.-21.10.2005, Congress Center Düsseldorf - Poster Session: Decontamination DEC-21
PT Konferenz-Poster
AB
A novel approach to the "in situ" study of organic matter is represented by LTA (Low Temperature Ashing) by non-equilibrium oxygen plasma coupled with other analytical techniques. The LTA technique destroys OM layer by layer with minimal disturbance to the mineral constituents. This disruption can be monitored by conventional or spectroscopic techniques before and after the treatment. This approach was used on all the insoluble products obtained by entrapment of a recombinant prion protein (recPrP) in a matrix of organo-mineral complexes, obtained by interaction between birnessite (Bir) and cathecol at two different concentration 3 and 5 mM (C3 and C5, respectively), to establish the degree of protection afforded by the matrix.
The presence of recPrP influenced both the kinetics and the extent of organic C removal as respect to the samples without protein and the effect was more pronounced when the protein was added during catechol polymerization. After 24 h-treatment for C3 and C5 samples the amount of removed C and N was about 91% for both. Only for Bir-C5-recPrP, when the protein was added during polymerization process) smaller removal of C (78%) and of N (68%) were measured, thus indicating a higher protection of the protein to the plasma oxidation.
In Bir-C3 complexes with recPrP added during or after catechol polymerization either after 5 h or 24 h of treatment the C removal from catechol and recPrP protein maintained a similar rate as time 0 to indicate that, at this cathecol concentration, the sample preparation did not affect the distribution of protein in the complex.
In Bir-C5 complexes only when protein was added after cathecol polymerization (Bir-C5+recPrP) the behavior after different treatments times was similar to the Bir-C3 complexes. When protein was added during catechol polymerization (Bir-C5-recPrP) the residual recPrP after all treatments resulted higher. This indicates a different interaction and distribution of recPrP in the complexes during polymerization processes such to to favor protection of the recPrP to LTA oxidation.
IN Wenn der pflanzliche Gerbstoff Catechin aus verrottenden Pflanzenteilen in Gegenwart von Prionprotein und dem nach dem schottischen Ort Birness genannten Manganoxid-Mineral Birnessit polymerisiert, dann wird das Prionprotein in die entstehenden Strukturen eingebaut und geschützt.
AD A.Pucci, L.Calamai, Dipartimento di Scienza del Suolo e Nutrizione della Pianta, Universita' di Firenze, Piazzale delle Cascine 28, 50144 Firenze, Italy; L.D'Acqui, Istituto per lo Studio degli Ecosistemi ISE-CNR, Via Madonna del Piano, 50019 Sesto Fiorentino, Italy; F.Russo, M.Rao, L.Gianfreda, Dipartimento di Scienze del Suolo, della Pianta e dell'Ambiente, Università degli Studi di Napoli Frederico II, Portici, Italy
SP englisch
PO Deutschland