| Autor: |
Thorsten Zerlin, Kay Frank, Kasischke, Nicole, Maggakis-Kelemen, Christina, Artmann, Aysegül Temiz, Porst, Dariusz, Kayser, Peter, Linder, Peter, Artmann, Gerhard Michael |
| Předmět: |
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| Zdroj: |
European Biophysics Journal; Dec2007, Vol. 37 Issue 1, p1-10, 10p, 1 Diagram, 3 Charts, 4 Graphs |
| Abstrakt: |
Human red blood cells (RBCs) exhibit sudden changes in their biophysical properties at body temperature ( T B). RBCs were seen to undergo a spontaneous transition from blockage to passage at T C = 36.4 ± 0.3°C, when the temperature dependency of RBC-passages through 1.3 μm narrow micropipettes was observed. Moreover, concentrated hemoglobin solutions (45 g/dl) showed a viscosity breakdown between 36 and 37°C. With human hemoglobin, a structural transition was observed at T B as circular dichroism (CD) experiments revealed. This leads to the assumption that a species’ body temperature occupies a unique position on the temperature scale and may even be imprinted in the structure of certain proteins. In this study, it was investigated whether hemoglobins of species with a T B different from those of human show temperature transitions and whether those were also linked to the species’ T B. The main conclusion was drawn from dynamic light scattering (DLS) and CD experiments. It was observed that such structural temperature transitions did occur in hemoglobins from all studied species and were correlated linearly (slope 0.81, r = 0.95) with the species’ body temperature. We presumed that α-helices of hemoglobin were able to unfold more readily around T B. α-helical unfolding would initiate molecular aggregation causing RBC passage and viscosity breakdown as mentioned above. Thus, structural molecular changes of hemoglobin could determine biophysical effects visible on a macroscopic scale. It is hypothesized that the species’ body temperature was imprinted into the structure of hemoglobins. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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