A922 Sequential measurement of 1 hour creatinine clearance (1-CRCL) in critically ill patients at risk of acute kidney injury (AKI)

Meeting abstrac

Food-grade sugar can promote differentiation in melon (Cucumis melo L.) tissue culture

The objective of the present study was to investigate the origin of discrepancy between experimental results in in vitro culture of Turkish melon (Cucumis melo L.) cultivars, conducted by the same individual using the same protocol and same seed batches in two different laboratories. The difference in the sucrose source was found to be the major reason for the deviation in results between the two laboratories. The percentage of regenerating explants and the number of bud-like protuberances and/or shoots were significantly greater when a food-grade Turkish sucrose was used in the medium compared with analytical-grade sucrose. Media formulated with the food-grade sucrose regenerated 37 and 67 % more explants and bud-like protuberances and/or shoots per explant, respectively, than media containing analytical-grade sucrose. No meaningful differences were found in added elements or anions between the sucrose sources or by liquid chromatography/mass spectroscopy. The only significant chemical difference observed between the sucrose samples was the presence of melanoidins (Maillard reaction products) in the food-grade sucrose. The melanoidins were of high molecular weight (>3,000 Da determined by ultrafiltration), with characteristic ultraviolet–visible spectra and in vitro antioxidant activity. Melanoidin-containing sucrose can be differentiated by color and spectroscopy

Glass Transition and Water Dynamics in Hyaluronic Acid Hydrogels

Glass transition and water dynamics in hydrated hyaluronic acid (HA) hydrogels crosslinked by divinyl sulfone (DVS) were studied by differential scanning calorimetry (DSC), dielectric relaxation spectroscopy (DRS) and water sorption-desorption (ESI) measurements. A critical water fraction of about h (w) = 0.17 (g of water per g of hydrated HA) for a change in the hydration properties of the material was estimated. Water crystallization was recorded by DSC during cooling and heating for water fraction values h (w) a parts per thousand yenaEuro parts per thousand 0.31. The glass transition of the hydrated system was recorded in the water fraction region 0.06 a parts per thousand currency signaEuro parts per thousand h (w) a parts per thousand currency signaEuro parts per thousand 0.59. The T (g) was found to decrease with increasing hydration level, starting from T (g) = -48 A degrees C down to about T (g) = -80 A degrees C and then to stabilize there, for the hydration levels where water crystallization occurs, suggesting that the origin of the glass transition is the combined motion of uncrystallized water molecules attached to primary hydration sites and segments of the HA chains. DRS studies revealed two relaxation peaks, associated with the main secondary relaxation process of uncrystallized water molecules (UCW) triggering the mobility of polar groups and the segmental mobility of HA chains (alpha relaxation). The alpha relaxation was in good agreement with the results by DSC. A qualitative change in the dynamics of the alpha relaxation was found for h (w) = 0.23 and was attributed to a reorganization of water in the material due to structural changes. Finally, the dielectric strength of the relaxation of UCW was found to decrease in the water fraction region of the structural changes, i.e. for h (w) similar to 0.23.Panagopoulou, A.; Vázquez Molina, J.; Kyritsis, A.; Monleón Pradas, M.; Vallés Lluch, A.; Gallego-Ferrer, G.; Pissis, P. (2013). Glass transition and water dynamics in hyaluronic acid hydrogels. Food Biophysics. 8(3):192-202. https://doi.org/10.1007/s11483-013-9295-219220283T.C. Laurent, Ciba Foundation Symposium, vol. 143 (John Wiley and Sons, New York, 1989), pp. 1–298J. Necas, L. Bartosikov, P. Brauner, J. Kolar, Vet. Med. 53(8), 397–411 (2008)M.K. Cowman, M. Li, E.A. Balazs, Biophys. J. 75, 2030–2037 (1998)M.K. Cowman, S. Matsuoka, Carbohydr. Res. 340, 791–809 (2005)C.E. Schanté, G. Zuber, C. Herlin, T.F. Vendamme, Carbohydr. Polym. 85, 469–489 (2011)E.J. Oh, K. Park, K.S. Kim, J. Kim, J.-A. Yang, J.-H. Kong, M.Y. Lee, A.S. Hoffman, S.K. Hahn, J. Control. Release 141, 2–12 (2010)A.S. Hoffman, Adv. Drug Deliv. Rev. 54, 3–12 (2002)F. Lee, M. Kurisawa, Acta Biomaterialia 9(2), 5143–5152 (2013)H.N. Joshi, E.M. Topp, Int. J. Pharm. 80, 213–225 (1992)J. Kucerik, A. Prusova, A. Rotaru, K. Flimel, J. Janecek, P. Conte, Thermochim. Acta 523, 245–249 (2011)M.N. Collins, C. Birkinshaw, J. Mater. Sci. Mater. Med. 19, 3335–3343 (2008)R. Servaty, J. Schiller, H. Binder, K. Arnold, Int. J. Biol. Macromol. 28, 121–127 (2001)J. Kaufmann, K. Möhle, H.J. Hofmann, K. Arnold, J. Mol. Struct. (THEOCHEM) 422, 109–121 (1998)H. Sugimoto, T. Miki, K. Κanayama, M. Norimoto, J. Non-Cryst. Solids 354, 3220–3224 (2008)J. Mijović, Y. Bian, R.A. Gross, B. Chen, Macromolecules 38, 10812–10819 (2005)J. Swenson, H. Jansson, J. Hedström, R. Bergman, J. Phys. Condens. Matter 19, 205109–205117 (2007)C. Gainaru, A. Fillmer, R. Böhmer, J. Phys. Chem. B 113, 12628–12631 (2009)W. Doster, S. Busch, A.M. Gaspar, M.S. Appavu, J. Wuttke, H. Scheer, Phys. Rev. Lett. 104, 098101–098104 (2010)A. Panagopoulou, A. Kyritsis, N. Shinyashiki, P. Pissis, J. Phys. Chem. B 116, 4593–4602 (2012)P. Pissis, A. Kyritsis, J. Polym. Sci. B Polym. Phys. 51(3), 159–175 (2013)G. Careri, Prog. Biophys. Mol. Biol. 70, 223–249 (1998)S. Cerveny, A. Alegria, J. Colmenero, Phys. Rev. E 77, 031803–031807 (2008)K.L. Ngai, S. Capaccioli, S. Ancherbak, N. Shinyashiki, Phil. Mag. 91, 1809–1835 (2011)A. Panagopoulou, A. Kyritsis, A.M. Aravantinou, D. Nanopoulos, R. Sabater i Serra, J.L. Gómez Ribellez, N. Shinyashiki, P. Pissis, Food Biophys. 6, 199–209 (2011)A. Panagopoulou, A. Kyritsis, R. Sabater i Serra, J.L. Gómez Ribellez, N. Shinyashiki, P. Pissis, Biochim. Biophys. Acta 1814, 1984–1996 (2011)R.B. Gregory, Protein-Solvent Interactions (Marcel Dekker, New York, USA, 1995)D. Ringe, G.A. Petsko, Biophys. Chem. 105, 667–680 (2003)P.W. Fenimore, H. Frauenfelder, B.H. McMahon, R.D. Young, Proc. Natl. Acad. Sci. 101, 14408–14413 (2004)Y. Miyazaki, T. Matsuo, H. Suga, J. Phys. Chem. B 104, 8044–8052 (2000)N. Shinyashiki, W. Yamamoto, A. Yokoyama, T. Yoshinari, S. Yagihara, K.L. Ngai, S. Capaccioli, J. Phys. Chem. B 113, 14448–14456 (2009)S. Khodadadi, A. Malkovskiy, A. Kisliuk, A.P. Sokolov, Biochim. Biophys. Acta 1804, 15–19 (2010)H. Jansson, J. Swenson, Biochim. Biophys. Acta 1804, 20–26 (2010)A.L. Tournier, J. Xu, J.C. Smith, Biophys. J. 85, 1871–1875 (2003)D. Porter, F. Vollrath, Biochim. Biophys. Acta 1824, 785–791 (2012)T. Vuletić, S. Dolanski Babić, T. Ivek, D. Grgičin, S. Tomić, Phys. Rev. E 82, 011922–011932 (2010)L. Greenspan, Humidity fixed points of binary saturated aqueous solutions. J. Res. Nat. Bur. Stand. A Phys. Chem. 81A, 89–96 (1977)F. Kremer, A. Schönhals (eds.), Broadband Dielectric Spectroscopy (Springer, Berlin, 2002)R.H. Cole, K.S. Cole, J. Chem. Phys. 10, 98–105 (1942)R.P. Chartoff, P.T. Weissman, A. Sirkar, in The Application of Dynamic Mechanical Methods to T g Determination in polymers: An overview, Assignment of the Glass Transition, ASTM STP 1249, ed. by R.J. Seyler (American Society for Testing and Materials, Philadelphia, 1994), pp. 88–107H. Vogel, Phys. Z. 22, 645–646 (1921)A. Anagnostopoulou-Konsta, P. Pissis, J. Phys. D. Appl. Phys. 20, 1168–1174 (1987)D. Daoukaki-Diamanti, P. Pissis, G. Boudouris, Chem. Phys. 91, 315–325 (1984)P. Pissis, J. Phys. D. Appl. Phys. 18, 1897–1908 (1985)S. Ratkovic, P. Pissis, J. Mater. Sci. 32, 3061–3068 (1997)P. Pissis, J. Exp. Bot 41, 677–684 (1990