TY - JOUR A1 - Bassam, Rasha A1 - Artmann, Gerhard A1 - Hescheler, Jürgen A1 - Graef, T. A1 - Temiz Artmann, Aysegül A1 - Porst, Dariusz A1 - Linder, Peter A1 - Kayser, Peter A1 - Arinkin, Vladimir A1 - Gossmann, Matthias A1 - Digel, Ilya T1 - Alterations in human hemoglobin structure related to red blood cell storage N2 - The importance of the availability of stored blood or blood cells, respectively, for urgent transfusion cannot be overestimated. Nowadays, blood storage becomes even more important since blood products are used for epidemiological studies, bio-technical research or banked for transfusion purposes. Thus blood samples must not only be processed, stored, and shipped to preserve their efficacy and safety, but also all parameters of storage must be recorded and reported for Quality Assurance. Therefore, blood banks and clinical research facilities are seeking more accurate, automated means for blood storage and blood processing. KW - Hämoglobin KW - Hämoglobinstruktur KW - Blutzellenlagerung KW - Hemoglobin structure KW - Red blood cell storage Y1 - 2011 ER - TY - JOUR A1 - Preiß, C. A1 - Linder, Peter A1 - Wendt, K. A1 - Krystek, M. A1 - Digel, Ilya A1 - Gossmann, Matthias A1 - Temiz Artmann, Aysegül A1 - Porst, Dariusz A1 - Kayser, Peter A1 - Bassam, Rasha A1 - Artmann, Gerhard T1 - Engineering technology for plant physiology and plant stress research N2 - Plant physiology and plant stress: Plant physiology will be much more important for human mankind because of yield and cultivation limits of crops determined by their resistance to stress. To assess and counteract various stress factors it is necessary to conduct plant research to gain information and results on plant physiology. KW - Pflanzenphysiologie KW - Pflanzenstress KW - Pflanzenscanner KW - plant stress KW - plant scanner Y1 - 2011 ER - TY - CHAP A1 - Bassam, Rasha A1 - Digel, Ilya A1 - Artmann, Gerhard T1 - Effect of nitric oxide on protein thermal stability : [abstract] N2 - As a deduction from these results, we can conclude that proteins mainly in vitro, denaturate totally at a temperature between 57°C -62°C, and they also affected by NO and different ions types. In which mainly, NO cause earlier protein denaturation, which means that, NO has a destabilizing effect on proteins, and also different ions will alter the protein denaturation in which, some ions will cause earlier protein denaturation while others not. KW - Stickstoffmonoxid KW - Proteine KW - Hämoglobin KW - nitric oxide gas KW - protein KW - hemoglobin Y1 - 2009 ER - TY - JOUR A1 - Bassam, Rasha A1 - Hescheler, Jürgen A1 - Temiz Artmann, Aysegül A1 - Artmann, Gerhard A1 - Digel, Ilya T1 - Effects of spermine NONOate and ATP on the thermal stability of hemoglobin JF - BMC Biophysics N2 - Background Minor changes in protein structure induced by small organic and inorganic molecules can result in significant metabolic effects. The effects can be even more profound if the molecular players are chemically active and present in the cell in considerable amounts. The aim of our study was to investigate effects of a nitric oxide donor (spermine NONOate), ATP and sodium/potassium environment on the dynamics of thermal unfolding of human hemoglobin (Hb). The effect of these molecules was examined by means of circular dichroism spectrometry (CD) in the temperature range between 25°C and 70°C. The alpha-helical content of buffered hemoglobin samples (0.1 mg/ml) was estimated via ellipticity change measurements at a heating rate of 1°C/min. Results Major results were: 1) spermine NONOate persistently decreased the hemoglobin unfolding temperature T u irrespectively of the Na + /K + environment, 2) ATP instead increased the unfolding temperature by 3°C in both sodium-based and potassium-based buffers and 3) mutual effects of ATP and NO were strongly influenced by particular buffer ionic compositions. Moreover, the presence of potassium facilitated a partial unfolding of alpha-helical structures even at room temperature. Conclusion The obtained data might shed more light on molecular mechanisms and biophysics involved in the regulation of protein activity by small solutes in the cell. KW - Nitric Oxide Donor KW - NONOate KW - Circular Dichroism KW - Nitric Oxide Y1 - 2012 U6 - http://dx.doi.org/10.1186/2046-1682-5-16 SN - 2046-1682 VL - 5 PB - BioMed Central CY - London ER - TY - JOUR A1 - Bassam, Rasha A1 - Digel, Ilya A1 - Hescheler, Jürgen A1 - Temiz Artmann, Aysegül A1 - Artmann, Gerhard T1 - Effects of spermine NONOate and ATP on protein aggregation: light scattering evidences JF - BMC Biophysics Y1 - 2013 U6 - http://nbn-resolving.de/urn/resolver.pl?10.1186/2046-1682-6-1 SN - 2046-1682 SP - 1 EP - 14 PB - BioMed Central CY - London ER - TY - CHAP A1 - Schlemmer, Katharina A1 - Porst, Dariusz A1 - Bassam, Rasha A1 - Artmann, Gerhard A1 - Digel, Ilya ED - Erni, Daniel ED - Fischerauer, Alice ED - Himmel, Jörg ED - Seeger, Thomas ED - Thelen, Klaus T1 - Effects of nitric oxide (NO) and ATP on red blood cell phenotype and deformability T2 - 2nd YRA MedTech Symposium 2017 : June 8th - 9th / 2017 / Hochschule Ruhr-West Y1 - 2017 SN - 978-3-9814801-9-1 U6 - http://dx.doi.org/10.17185/duepublico/43984 N1 - A young researchers track of the 7th IEEE Workshop & SENSORICA 2017 SP - 100 EP - 101 PB - Universität Duisburg-Essen CY - Duisburg ER - TY - THES A1 - Bassam Abduljabbar, Rasha T1 - Physikalisch-chemische Steuerung der Proteinstabilität in biologischen Systemen T1 - Physico-chemical management of protein stability in biological systems Y1 - 2015 ER -